[{"ddc":["616"],"date_created":"2021-10-07T09:13:29Z","article_type":"original","corr_author":"1","pmid":1,"keyword":["virology","infectious diseases"],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_number":"1853","volume":13,"has_accepted_license":"1","title":"A structural perspective of the role of IP6 in immature and mature retroviral assembly","quality_controlled":"1","license":"https://creativecommons.org/licenses/by/4.0/","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"status":"public","intvolume":"        13","author":[{"first_name":"Martin","full_name":"Obr, Martin","last_name":"Obr","orcid":"0000-0003-1756-6564","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur","orcid":"0000-0003-4790-8078"},{"first_name":"Robert A.","full_name":"Dick, Robert A.","last_name":"Dick"}],"external_id":{"pmid":["34578434"],"isi":["000699841100001"]},"language":[{"iso":"eng"}],"article_processing_charge":"Yes","project":[{"call_identifier":"FWF","grant_number":"P31445","_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid"}],"publication_status":"published","file":[{"file_id":"10115","access_level":"open_access","creator":"cchlebak","date_created":"2021-10-08T10:38:15Z","relation":"main_file","content_type":"application/pdf","file_name":"2021_Viruses_Obr.pdf","checksum":"bcfd72a12977d48e22df3d0cc55aacf1","file_size":4146796,"success":1,"date_updated":"2021-10-08T10:38:15Z"}],"oa_version":"Published Version","month":"09","isi":1,"date_updated":"2025-04-15T08:24:49Z","year":"2021","abstract":[{"text":"The small cellular molecule inositol hexakisphosphate (IP6) has been known for ~20 years to promote the in vitro assembly of HIV-1 into immature virus-like particles. However, the molecular details underlying this effect have been determined only recently, with the identification of the IP6 binding site in the immature Gag lattice. IP6 also promotes formation of the mature capsid protein (CA) lattice via a second IP6 binding site, and enhances core stability, creating a favorable environment for reverse transcription. IP6 also enhances assembly of other retroviruses, from both the Lentivirus and the Alpharetrovirus genera. These findings suggest that IP6 may have a conserved function throughout the family Retroviridae. Here, we discuss the different steps in the viral life cycle that are influenced by IP6, and describe in detail how IP6 interacts with the immature and mature lattices of different retroviruses.","lang":"eng"}],"scopus_import":"1","publisher":"MDPI","date_published":"2021-09-17T00:00:00Z","publication":"Viruses","issue":"9","file_date_updated":"2021-10-08T10:38:15Z","day":"17","_id":"10103","publication_identifier":{"issn":["1999-4915"]},"acknowledgement":"We thank Volker M. Vogt for his critical comments in preparation of the review.","doi":"10.3390/v13091853","citation":{"ieee":"M. Obr, F. K. Schur, and R. A. Dick, “A structural perspective of the role of IP6 in immature and mature retroviral assembly,” <i>Viruses</i>, vol. 13, no. 9. MDPI, 2021.","chicago":"Obr, Martin, Florian KM Schur, and Robert A. Dick. “A Structural Perspective of the Role of IP6 in Immature and Mature Retroviral Assembly.” <i>Viruses</i>. MDPI, 2021. <a href=\"https://doi.org/10.3390/v13091853\">https://doi.org/10.3390/v13091853</a>.","ama":"Obr M, Schur FK, Dick RA. A structural perspective of the role of IP6 in immature and mature retroviral assembly. <i>Viruses</i>. 2021;13(9). doi:<a href=\"https://doi.org/10.3390/v13091853\">10.3390/v13091853</a>","mla":"Obr, Martin, et al. “A Structural Perspective of the Role of IP6 in Immature and Mature Retroviral Assembly.” <i>Viruses</i>, vol. 13, no. 9, 1853, MDPI, 2021, doi:<a href=\"https://doi.org/10.3390/v13091853\">10.3390/v13091853</a>.","short":"M. Obr, F.K. Schur, R.A. Dick, Viruses 13 (2021).","apa":"Obr, M., Schur, F. K., &#38; Dick, R. A. (2021). A structural perspective of the role of IP6 in immature and mature retroviral assembly. <i>Viruses</i>. MDPI. <a href=\"https://doi.org/10.3390/v13091853\">https://doi.org/10.3390/v13091853</a>","ista":"Obr M, Schur FK, Dick RA. 2021. A structural perspective of the role of IP6 in immature and mature retroviral assembly. Viruses. 13(9), 1853."},"department":[{"_id":"FlSc"}],"type":"journal_article","oa":1},{"has_accepted_license":"1","related_material":{"record":[{"relation":"software","status":"public","id":"14502"}]},"volume":213,"keyword":["Structural Biology"],"article_number":"107808","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["572"],"date_created":"2021-11-15T12:21:42Z","article_type":"original","corr_author":"1","external_id":{"isi":["000720259500002"]},"author":[{"orcid":"0000-0001-8370-6161","last_name":"Dimchev","first_name":"Georgi A","full_name":"Dimchev, Georgi A","id":"38C393BE-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Amiri","full_name":"Amiri, Behnam","first_name":"Behnam"},{"last_name":"Fäßler","orcid":"0000-0001-7149-769X","first_name":"Florian","full_name":"Fäßler, Florian","id":"404F5528-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Martin","full_name":"Falcke, Martin","last_name":"Falcke"},{"first_name":"Florian KM","full_name":"Schur, Florian KM","orcid":"0000-0003-4790-8078","last_name":"Schur","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}],"language":[{"iso":"eng"}],"status":"public","intvolume":"       213","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"title":"Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data","quality_controlled":"1","publisher":"Elsevier ","date_published":"2021-11-03T00:00:00Z","isi":1,"month":"11","date_updated":"2025-04-15T08:25:41Z","year":"2021","abstract":[{"lang":"eng","text":"A precise quantitative description of the ultrastructural characteristics underlying biological mechanisms is often key to their understanding. This is particularly true for dynamic extra- and intracellular filamentous assemblies, playing a role in cell motility, cell integrity, cytokinesis, tissue formation and maintenance. For example, genetic manipulation or modulation of actin regulatory proteins frequently manifests in changes of the morphology, dynamics, and ultrastructural architecture of actin filament-rich cell peripheral structures, such as lamellipodia or filopodia. However, the observed ultrastructural effects often remain subtle and require sufficiently large datasets for appropriate quantitative analysis. The acquisition of such large datasets has been enabled by recent advances in high-throughput cryo-electron tomography (cryo-ET) methods. This also necessitates the development of complementary approaches to maximize the extraction of relevant biological information. We have developed a computational toolbox for the semi-automatic quantification of segmented and vectorized filamentous networks from pre-processed cryo-electron tomograms, facilitating the analysis and cross-comparison of multiple experimental conditions. GUI-based components simplify the processing of data and allow users to obtain a large number of ultrastructural parameters describing filamentous assemblies. We demonstrate the feasibility of this workflow by analyzing cryo-ET data of untreated and chemically perturbed branched actin filament networks and that of parallel actin filament arrays. In principle, the computational toolbox presented here is applicable for data analysis comprising any type of filaments in regular (i.e. parallel) or random arrangement. We show that it can ease the identification of key differences between experimental groups and facilitate the in-depth analysis of ultrastructural data in a time-efficient manner."}],"scopus_import":"1","oa_version":"Published Version","file":[{"checksum":"6b209e4d44775d4e02b50f78982c15fa","file_name":"2021_JournalStructBiol_Dimchev.pdf","content_type":"application/pdf","success":1,"date_updated":"2021-11-15T13:11:27Z","file_size":16818304,"file_id":"10291","relation":"main_file","date_created":"2021-11-15T13:11:27Z","creator":"cchlebak","access_level":"open_access"}],"article_processing_charge":"Yes (via OA deal)","project":[{"name":"Structure and isoform diversity of the Arp2/3 complex","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","grant_number":"P33367"},{"name":"Protein structure and function in filopodia across scales","_id":"2674F658-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","grant_number":"M02495"}],"publication_status":"published","citation":{"ama":"Dimchev GA, Amiri B, Fäßler F, Falcke M, Schur FK. Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data. <i>Journal of Structural Biology</i>. 2021;213(4). doi:<a href=\"https://doi.org/10.1016/j.jsb.2021.107808\">10.1016/j.jsb.2021.107808</a>","mla":"Dimchev, Georgi A., et al. “Computational Toolbox for Ultrastructural Quantitative Analysis of Filament Networks in Cryo-ET Data.” <i>Journal of Structural Biology</i>, vol. 213, no. 4, 107808, Elsevier , 2021, doi:<a href=\"https://doi.org/10.1016/j.jsb.2021.107808\">10.1016/j.jsb.2021.107808</a>.","short":"G.A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, F.K. Schur, Journal of Structural Biology 213 (2021).","ista":"Dimchev GA, Amiri B, Fäßler F, Falcke M, Schur FK. 2021. Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data. Journal of Structural Biology. 213(4), 107808.","apa":"Dimchev, G. A., Amiri, B., Fäßler, F., Falcke, M., &#38; Schur, F. K. (2021). Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data. <i>Journal of Structural Biology</i>. Elsevier . <a href=\"https://doi.org/10.1016/j.jsb.2021.107808\">https://doi.org/10.1016/j.jsb.2021.107808</a>","ieee":"G. A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, and F. K. Schur, “Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data,” <i>Journal of Structural Biology</i>, vol. 213, no. 4. Elsevier , 2021.","chicago":"Dimchev, Georgi A, Behnam Amiri, Florian Fäßler, Martin Falcke, and Florian KM Schur. “Computational Toolbox for Ultrastructural Quantitative Analysis of Filament Networks in Cryo-ET Data.” <i>Journal of Structural Biology</i>. Elsevier , 2021. <a href=\"https://doi.org/10.1016/j.jsb.2021.107808\">https://doi.org/10.1016/j.jsb.2021.107808</a>."},"type":"journal_article","department":[{"_id":"FlSc"}],"oa":1,"publication_identifier":{"issn":["1047-8477"]},"acknowledgement":"This research was supported by the Scientific Service Units (SSUs) of IST Austria through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), the BioImaging Facility (BIF), and the Electron Microscopy Facility (EMF). We also thank Victor-Valentin Hodirnau for help with cryo-ET data acquisition. The authors acknowledge support from IST Austria and from the Austrian Science Fund (FWF): M02495 to G.D. and Austrian Science Fund (FWF): P33367 to F.K.M.S.","doi":"10.1016/j.jsb.2021.107808","_id":"10290","day":"03","publication":"Journal of Structural Biology","issue":"4","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"Bio"},{"_id":"EM-Fac"}],"file_date_updated":"2021-11-15T13:11:27Z"},{"has_accepted_license":"1","volume":12,"related_material":{"link":[{"relation":"press_release","description":"News on IST Homepage","url":"https://ist.ac.at/en/news/how-retroviruses-become-infectious/"}]},"article_number":"3226","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"corr_author":"1","article_type":"original","date_created":"2021-05-28T14:25:50Z","ddc":["570"],"language":[{"iso":"eng"}],"author":[{"full_name":"Obr, Martin","first_name":"Martin","orcid":"0000-0003-1756-6564","last_name":"Obr","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Ricana","first_name":"Clifton L.","full_name":"Ricana, Clifton L."},{"first_name":"Nadia","full_name":"Nikulin, Nadia","last_name":"Nikulin"},{"last_name":"Feathers","first_name":"Jon-Philip R.","full_name":"Feathers, Jon-Philip R."},{"last_name":"Klanschnig","full_name":"Klanschnig, Marco","first_name":"Marco"},{"id":"3A18A7B8-F248-11E8-B48F-1D18A9856A87","full_name":"Thader, Andreas","first_name":"Andreas","last_name":"Thader"},{"last_name":"Johnson","first_name":"Marc C.","full_name":"Johnson, Marc C."},{"first_name":"Volker M.","full_name":"Vogt, Volker M.","last_name":"Vogt"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","last_name":"Schur","full_name":"Schur, Florian KM","first_name":"Florian KM"},{"full_name":"Dick, Robert A.","first_name":"Robert A.","last_name":"Dick"}],"external_id":{"isi":["000659145000011"]},"intvolume":"        12","status":"public","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"quality_controlled":"1","title":"Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer","date_published":"2021-05-28T00:00:00Z","publisher":"Nature Research","year":"2021","abstract":[{"lang":"eng","text":"Inositol hexakisphosphate (IP6) is an assembly cofactor for HIV-1. We report here that IP6 is also used for assembly of Rous sarcoma virus (RSV), a retrovirus from a different genus. IP6 is ~100-fold more potent at promoting RSV mature capsid protein (CA) assembly than observed for HIV-1 and removal of IP6 in cells reduces infectivity by 100-fold. Here, visualized by cryo-electron tomography and subtomogram averaging, mature capsid-like particles show an IP6-like density in the CA hexamer, coordinated by rings of six lysines and six arginines. Phosphate and IP6 have opposing effects on CA in vitro assembly, inducing formation of T = 1 icosahedrons and tubes, respectively, implying that phosphate promotes pentamer and IP6 hexamer formation. Subtomogram averaging and classification optimized for analysis of pleomorphic retrovirus particles reveal that the heterogeneity of mature RSV CA polyhedrons results from an unexpected, intrinsic CA hexamer flexibility. In contrast, the CA pentamer forms rigid units organizing the local architecture. These different features of hexamers and pentamers determine the structural mechanism to form CA polyhedrons of variable shape in mature RSV particles."}],"scopus_import":"1","date_updated":"2025-04-15T08:24:49Z","isi":1,"month":"05","file":[{"relation":"main_file","date_created":"2021-06-09T15:21:14Z","creator":"kschuh","access_level":"open_access","file_id":"9538","success":1,"date_updated":"2021-06-09T15:21:14Z","file_size":6166295,"checksum":"53ccc53d09a9111143839dbe7784e663","file_name":"2021_NatureCommunications_Obr.pdf","content_type":"application/pdf"}],"oa_version":"Published Version","publication_status":"published","project":[{"call_identifier":"FWF","grant_number":"P31445","_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid"}],"article_processing_charge":"No","oa":1,"department":[{"_id":"FlSc"}],"type":"journal_article","citation":{"ieee":"M. Obr <i>et al.</i>, “Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer,” <i>Nature Communications</i>, vol. 12, no. 1. Nature Research, 2021.","chicago":"Obr, Martin, Clifton L. Ricana, Nadia Nikulin, Jon-Philip R. Feathers, Marco Klanschnig, Andreas Thader, Marc C. Johnson, Volker M. Vogt, Florian KM Schur, and Robert A. Dick. “Structure of the Mature Rous Sarcoma Virus Lattice Reveals a Role for IP6 in the Formation of the Capsid Hexamer.” <i>Nature Communications</i>. Nature Research, 2021. <a href=\"https://doi.org/10.1038/s41467-021-23506-0\">https://doi.org/10.1038/s41467-021-23506-0</a>.","short":"M. Obr, C.L. Ricana, N. Nikulin, J.-P.R. Feathers, M. Klanschnig, A. Thader, M.C. Johnson, V.M. Vogt, F.K. Schur, R.A. Dick, Nature Communications 12 (2021).","ama":"Obr M, Ricana CL, Nikulin N, et al. Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer. <i>Nature Communications</i>. 2021;12(1). doi:<a href=\"https://doi.org/10.1038/s41467-021-23506-0\">10.1038/s41467-021-23506-0</a>","mla":"Obr, Martin, et al. “Structure of the Mature Rous Sarcoma Virus Lattice Reveals a Role for IP6 in the Formation of the Capsid Hexamer.” <i>Nature Communications</i>, vol. 12, no. 1, 3226, Nature Research, 2021, doi:<a href=\"https://doi.org/10.1038/s41467-021-23506-0\">10.1038/s41467-021-23506-0</a>.","ista":"Obr M, Ricana CL, Nikulin N, Feathers J-PR, Klanschnig M, Thader A, Johnson MC, Vogt VM, Schur FK, Dick RA. 2021. Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer. Nature Communications. 12(1), 3226.","apa":"Obr, M., Ricana, C. L., Nikulin, N., Feathers, J.-P. R., Klanschnig, M., Thader, A., … Dick, R. A. (2021). Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer. <i>Nature Communications</i>. Nature Research. <a href=\"https://doi.org/10.1038/s41467-021-23506-0\">https://doi.org/10.1038/s41467-021-23506-0</a>"},"doi":"10.1038/s41467-021-23506-0","acknowledgement":"This work was funded by the National Institute of Allergy and Infectious Diseases under awards R01AI147890 to R.A.D., R01AI150454 to V.M.V, R35GM136258 in support of J-P.R.F, and the Austrian Science Fund (FWF) grant P31445 to F.K.M.S. Access to high-resolution cryo-ET data acquisition at EMBL Heidelberg was supported by iNEXT (grant no. 653706), funded by the Horizon 2020 program of the European Union (PID 4246). We thank Wim Hagen and Felix Weis at EMBL Heidelberg for support in cryo-ET data acquisition. This work made use of the Cornell Center for Materials Research Shared Facilities, which are supported through the NSF MRSEC program (DMR-179875). This research was also supported by the Scientific Service Units (SSUs) of IST Austria through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), and the Electron Microscopy Facility (EMF).","publication_identifier":{"eissn":["2041-1723"]},"_id":"9431","day":"28","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"EM-Fac"}],"file_date_updated":"2021-06-09T15:21:14Z","issue":"1","publication":"Nature Communications"},{"oa_version":"Published Version","file":[{"creator":"kschuh","access_level":"open_access","relation":"main_file","date_created":"2021-05-28T12:39:43Z","file_id":"9430","file_size":9358599,"success":1,"date_updated":"2021-05-28T12:39:43Z","content_type":"application/pdf","checksum":"337e0f7959c35ec959984cacdcb472ba","file_name":"2021_NatureCommunications_Morandell.pdf"}],"publication_status":"published","article_processing_charge":"No","project":[{"name":"ISTplus - Postdoctoral Fellowships","_id":"260C2330-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","grant_number":"754411"},{"_id":"25444568-B435-11E9-9278-68D0E5697425","name":"Probing the Reversibility of Autism Spectrum Disorders by Employing in vivo and in vitro Models","call_identifier":"H2020","grant_number":"715508"},{"name":"Molecular Drug Targets","_id":"2548AE96-B435-11E9-9278-68D0E5697425","grant_number":"W1232","call_identifier":"FWF"},{"grant_number":"F7807","name":"Stem Cell Modulation in Neural Development and Regeneration/ P07-Neural stem cells in autism and epilepsy","_id":"05A0D778-7A3F-11EA-A408-12923DDC885E"},{"_id":"265CB4D0-B435-11E9-9278-68D0E5697425","name":"Optical control of synaptic function via adhesion molecules","call_identifier":"FWF","grant_number":"I03600"}],"date_published":"2021-05-24T00:00:00Z","publisher":"Springer Nature","scopus_import":"1","abstract":[{"lang":"eng","text":"De novo loss of function mutations in the ubiquitin ligase-encoding gene Cullin3 lead to autism spectrum disorder (ASD). In mouse, constitutive haploinsufficiency leads to motor coordination deficits as well as ASD-relevant social and cognitive impairments. However, induction of Cul3 haploinsufficiency later in life does not lead to ASD-relevant behaviors, pointing to an important role of Cul3 during a critical developmental window. Here we show that Cul3 is essential to regulate neuronal migration and, therefore, constitutive Cul3 heterozygous mutant mice display cortical lamination abnormalities. At the molecular level, we found that Cul3 controls neuronal migration by tightly regulating the amount of Plastin3 (Pls3), a previously unrecognized player of neural migration. Furthermore, we found that Pls3 cell-autonomously regulates cell migration by regulating actin cytoskeleton organization, and its levels are inversely proportional to neural migration speed. Finally, we provide evidence that cellular phenotypes associated with autism-linked gene haploinsufficiency can be rescued by transcriptional activation of the intact allele in vitro, offering a proof of concept for a potential therapeutic approach for ASDs."}],"year":"2021","date_updated":"2026-06-16T22:31:03Z","isi":1,"month":"05","_id":"9429","day":"24","acknowledged_ssus":[{"_id":"PreCl"}],"file_date_updated":"2021-05-28T12:39:43Z","issue":"1","publication":"Nature Communications","oa":1,"type":"journal_article","department":[{"_id":"GaNo"},{"_id":"JoDa"},{"_id":"FlSc"},{"_id":"MiSi"},{"_id":"LifeSc"},{"_id":"Bio"}],"citation":{"mla":"Morandell, Jasmin, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>Nature Communications</i>, vol. 12, no. 1, 3058, Springer Nature, 2021, doi:<a href=\"https://doi.org/10.1038/s41467-021-23123-x\">10.1038/s41467-021-23123-x</a>.","ama":"Morandell J, Schwarz LA, Basilico B, et al. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>Nature Communications</i>. 2021;12(1). doi:<a href=\"https://doi.org/10.1038/s41467-021-23123-x\">10.1038/s41467-021-23123-x</a>","short":"J. Morandell, L.A. Schwarz, B. Basilico, S. Tasciyan, G.A. Dimchev, A. Nicolas, C.M. Sommer, C. Kreuzinger, C. Dotter, L. Knaus, Z. Dobler, E. Cacci, F.K. Schur, J.G. Danzl, G. Novarino, Nature Communications 12 (2021).","ista":"Morandell J, Schwarz LA, Basilico B, Tasciyan S, Dimchev GA, Nicolas A, Sommer CM, Kreuzinger C, Dotter C, Knaus L, Dobler Z, Cacci E, Schur FK, Danzl JG, Novarino G. 2021. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. Nature Communications. 12(1), 3058.","apa":"Morandell, J., Schwarz, L. A., Basilico, B., Tasciyan, S., Dimchev, G. A., Nicolas, A., … Novarino, G. (2021). Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-021-23123-x\">https://doi.org/10.1038/s41467-021-23123-x</a>","ieee":"J. Morandell <i>et al.</i>, “Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development,” <i>Nature Communications</i>, vol. 12, no. 1. Springer Nature, 2021.","chicago":"Morandell, Jasmin, Lena A Schwarz, Bernadette Basilico, Saren Tasciyan, Georgi A Dimchev, Armel Nicolas, Christoph M Sommer, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>Nature Communications</i>. Springer Nature, 2021. <a href=\"https://doi.org/10.1038/s41467-021-23123-x\">https://doi.org/10.1038/s41467-021-23123-x</a>."},"doi":"10.1038/s41467-021-23123-x","publication_identifier":{"eissn":["2041-1723"]},"acknowledgement":"We thank A. Coll Manzano, F. Freeman, M. Ladron de Guevara, and A. Ç. Yahya for technical assistance, S. Deixler, A. Lepold, and A. Schlerka for the management of our animal colony, as well as M. Schunn and the Preclinical Facility team for technical assistance. We thank K. Heesom and her team at the University of Bristol Proteomics Facility for the proteomics sample preparation, data generation, and analysis support. We thank Y. B. Simon for kindly providing the plasmid for lentiviral labeling. Further, we thank M. Sixt for his advice regarding cell migration and the fruitful discussions. This work was supported by the ISTPlus postdoctoral fellowship (Grant Agreement No. 754411) to B.B., by the European Union’s Horizon 2020 research and innovation program (ERC) grant 715508 (REVERSEAUTISM), and by the Austrian Science Fund (FWF) to G.N. (DK W1232-B24 and SFB F7807-B) and to J.G.D (I3600-B27).","article_number":"3058","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","keyword":["General Biochemistry","Genetics and Molecular Biology"],"corr_author":"1","article_type":"original","date_created":"2021-05-28T11:49:46Z","ddc":["572"],"has_accepted_license":"1","volume":12,"related_material":{"link":[{"relation":"press_release","url":"https://ist.ac.at/en/news/defective-gene-slows-down-brain-cells/"}],"record":[{"id":"19557","status":"public","relation":"dissertation_contains"},{"status":"public","relation":"earlier_version","id":"7800"},{"status":"public","relation":"dissertation_contains","id":"12401"}]},"ec_funded":1,"tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"quality_controlled":"1","title":"Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development","language":[{"iso":"eng"}],"external_id":{"isi":["000658769900010"]},"author":[{"first_name":"Jasmin","full_name":"Morandell, Jasmin","last_name":"Morandell","id":"4739D480-F248-11E8-B48F-1D18A9856A87"},{"id":"29A8453C-F248-11E8-B48F-1D18A9856A87","first_name":"Lena A","full_name":"Schwarz, Lena A","last_name":"Schwarz"},{"id":"36035796-5ACA-11E9-A75E-7AF2E5697425","first_name":"Bernadette","full_name":"Basilico, Bernadette","orcid":"0000-0003-1843-3173","last_name":"Basilico"},{"id":"4323B49C-F248-11E8-B48F-1D18A9856A87","last_name":"Tasciyan","orcid":"0000-0003-1671-393X","full_name":"Tasciyan, Saren","first_name":"Saren"},{"id":"38C393BE-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-8370-6161","last_name":"Dimchev","first_name":"Georgi A","full_name":"Dimchev, Georgi A"},{"id":"2A103192-F248-11E8-B48F-1D18A9856A87","full_name":"Nicolas, Armel","first_name":"Armel","last_name":"Nicolas"},{"id":"4DF26D8C-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1216-9105","last_name":"Sommer","full_name":"Sommer, Christoph M","first_name":"Christoph M"},{"last_name":"Kreuzinger","full_name":"Kreuzinger, Caroline","first_name":"Caroline","id":"382077BA-F248-11E8-B48F-1D18A9856A87"},{"id":"4C66542E-F248-11E8-B48F-1D18A9856A87","first_name":"Christoph","full_name":"Dotter, Christoph","orcid":"0000-0002-9033-9096","last_name":"Dotter"},{"first_name":"Lisa","full_name":"Knaus, Lisa","last_name":"Knaus","id":"3B2ABCF4-F248-11E8-B48F-1D18A9856A87"},{"id":"D23090A2-9057-11EA-883A-A8396FC7A38F","full_name":"Dobler, Zoe","first_name":"Zoe","last_name":"Dobler"},{"full_name":"Cacci, Emanuele","first_name":"Emanuele","last_name":"Cacci"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","first_name":"Florian KM"},{"full_name":"Danzl, Johann G","first_name":"Johann G","last_name":"Danzl","orcid":"0000-0001-8559-3973","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87"},{"id":"3E57A680-F248-11E8-B48F-1D18A9856A87","full_name":"Novarino, Gaia","first_name":"Gaia","last_name":"Novarino","orcid":"0000-0002-7673-7178"}],"intvolume":"        12","status":"public"},{"file":[{"date_created":"2023-11-22T14:58:44Z","relation":"main_file","access_level":"open_access","creator":"fschur","file_id":"14593","success":1,"date_updated":"2023-11-22T14:58:44Z","file_size":49297,"file_name":"3Dprint-files_download_v2.zip","checksum":"0108616e2a59e51879ea51299a29b091","content_type":"application/zip"},{"date_created":"2023-12-01T10:39:59Z","relation":"main_file","access_level":"open_access","creator":"cchlebak","file_id":"14637","date_updated":"2023-12-01T10:39:59Z","success":1,"file_size":641,"file_name":"readme.txt","checksum":"4c66ddedee4d01c1c4a7978208350cfc","content_type":"text/plain"}],"oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","contributor":[{"first_name":"Florian","contributor_type":"researcher","last_name":"Fäßler","orcid":"0000-0001-7149-769X","id":"404F5528-F248-11E8-B48F-1D18A9856A87"},{"id":"45FD126C-F248-11E8-B48F-1D18A9856A87","first_name":"Bettina","contributor_type":"researcher","last_name":"Zens"},{"id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","last_name":"Hauschild","first_name":"Robert","contributor_type":"researcher"},{"contributor_type":"researcher","first_name":"Florian KM","orcid":"0000-0003-4790-8078","last_name":"Schur","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}],"corr_author":"1","date_created":"2023-11-22T15:00:57Z","article_processing_charge":"No","project":[{"_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","name":"Structure and isoform diversity of the Arp2/3 complex","grant_number":"P33367"}],"ddc":["570"],"date_published":"2020-12-01T00:00:00Z","has_accepted_license":"1","publisher":"Institute of Science and Technology Austria","abstract":[{"text":"Cryo-electron microscopy (cryo-EM) of cellular specimens provides insights into biological processes and structures within a native context. However, a major challenge still lies in the efficient and reproducible preparation of adherent cells for subsequent cryo-EM analysis. This is due to the sensitivity of many cellular specimens to the varying seeding and culturing conditions required for EM experiments, the often limited amount of cellular material and also the fragility of EM grids and their substrate. Here, we present low-cost and reusable 3D printed grid holders, designed to improve specimen preparation when culturing challenging cellular samples directly on grids. The described grid holders increase cell culture reproducibility and throughput, and reduce the resources required for cell culturing. We show that grid holders can be integrated into various cryo-EM workflows, including micro-patterning approaches to control cell seeding on grids, and for generating samples for cryo-focused ion beam milling and cryo-electron tomography experiments. Their adaptable design allows for the generation of specialized grid holders customized to a large variety of applications.","lang":"eng"}],"year":"2020","related_material":{"record":[{"id":"8586","status":"public","relation":"research_data"}]},"date_updated":"2025-06-12T07:35:28Z","month":"12","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","image":"/images/cc_by_nc_sa.png","short":"CC BY-NC-SA (4.0)","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)"},"_id":"14592","day":"01","file_date_updated":"2023-12-01T10:39:59Z","license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","title":"STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy","oa":1,"author":[{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","first_name":"Florian KM"}],"citation":{"short":"F.K. Schur, (2020).","mla":"Schur, Florian KM. <i>STL-Files for 3D-Printed Grid Holders Described in  Fäßler F, Zens B, et Al.; 3D Printed Cell Culture Grid Holders for Improved Cellular Specimen Preparation in Cryo-Electron Microscopy</i>. Institute of Science and Technology Austria, 2020, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:14592\">10.15479/AT:ISTA:14592</a>.","ama":"Schur FK. STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy. 2020. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:14592\">10.15479/AT:ISTA:14592</a>","apa":"Schur, F. K. (2020). STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:14592\">https://doi.org/10.15479/AT:ISTA:14592</a>","ista":"Schur FK. 2020. STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:14592\">10.15479/AT:ISTA:14592</a>.","ieee":"F. K. Schur, “STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy.” Institute of Science and Technology Austria, 2020.","chicago":"Schur, Florian KM. “STL-Files for 3D-Printed Grid Holders Described in  Fäßler F, Zens B, et Al.; 3D Printed Cell Culture Grid Holders for Improved Cellular Specimen Preparation in Cryo-Electron Microscopy.” Institute of Science and Technology Austria, 2020. <a href=\"https://doi.org/10.15479/AT:ISTA:14592\">https://doi.org/10.15479/AT:ISTA:14592</a>."},"department":[{"_id":"FlSc"}],"type":"research_data","doi":"10.15479/AT:ISTA:14592","status":"public"},{"date_published":"2020-08-01T00:00:00Z","publisher":"Oxford University Press","date_updated":"2024-10-09T21:08:43Z","month":"08","volume":26,"year":"2020","oa_version":"None","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["Instrumentation"],"article_processing_charge":"No","date_created":"2024-04-03T09:40:11Z","publication_status":"published","corr_author":"1","article_type":"original","department":[{"_id":"FlSc"},{"_id":"EM-Fac"}],"type":"journal_article","citation":{"chicago":"Fäßler, Florian, Georgi A Dimchev, Victor-Valentin Hodirnau, Bettina Zens, Christoph Möhl, Frank Bradke, and Florian KM Schur. “Cryo-Electron Tomography Workflows for Quantitative Analysis of Actin Networks Involved in Cell Migration.” <i>Microscopy and Microanalysis</i>. Oxford University Press, 2020. <a href=\"https://doi.org/10.1017/s1431927620021881\">https://doi.org/10.1017/s1431927620021881</a>.","ieee":"F. Fäßler <i>et al.</i>, “Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration,” <i>Microscopy and Microanalysis</i>, vol. 26, no. S2. Oxford University Press, pp. 2518–2519, 2020.","ista":"Fäßler F, Dimchev GA, Hodirnau V-V, Zens B, Möhl C, Bradke F, Schur FK. 2020. Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration. Microscopy and Microanalysis. 26(S2), 2518–2519.","apa":"Fäßler, F., Dimchev, G. A., Hodirnau, V.-V., Zens, B., Möhl, C., Bradke, F., &#38; Schur, F. K. (2020). Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration. <i>Microscopy and Microanalysis</i>. Oxford University Press. <a href=\"https://doi.org/10.1017/s1431927620021881\">https://doi.org/10.1017/s1431927620021881</a>","ama":"Fäßler F, Dimchev GA, Hodirnau V-V, et al. Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration. <i>Microscopy and Microanalysis</i>. 2020;26(S2):2518-2519. doi:<a href=\"https://doi.org/10.1017/s1431927620021881\">10.1017/s1431927620021881</a>","mla":"Fäßler, Florian, et al. “Cryo-Electron Tomography Workflows for Quantitative Analysis of Actin Networks Involved in Cell Migration.” <i>Microscopy and Microanalysis</i>, vol. 26, no. S2, Oxford University Press, 2020, pp. 2518–19, doi:<a href=\"https://doi.org/10.1017/s1431927620021881\">10.1017/s1431927620021881</a>.","short":"F. Fäßler, G.A. Dimchev, V.-V. Hodirnau, B. Zens, C. Möhl, F. Bradke, F.K. Schur, Microscopy and Microanalysis 26 (2020) 2518–2519."},"language":[{"iso":"eng"}],"author":[{"full_name":"Fäßler, Florian","first_name":"Florian","orcid":"0000-0001-7149-769X","last_name":"Fäßler","id":"404F5528-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Dimchev, Georgi A","first_name":"Georgi A","last_name":"Dimchev","orcid":"0000-0001-8370-6161","id":"38C393BE-F248-11E8-B48F-1D18A9856A87"},{"id":"3661B498-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-3904-947X","last_name":"Hodirnau","full_name":"Hodirnau, Victor-Valentin","first_name":"Victor-Valentin"},{"id":"45FD126C-F248-11E8-B48F-1D18A9856A87","first_name":"Bettina","full_name":"Zens, Bettina","last_name":"Zens","orcid":"0000-0002-9561-1239"},{"full_name":"Möhl, Christoph","first_name":"Christoph","last_name":"Möhl"},{"last_name":"Bradke","first_name":"Frank","full_name":"Bradke, Frank"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur","orcid":"0000-0003-4790-8078","first_name":"Florian KM","full_name":"Schur, Florian KM"}],"status":"public","doi":"10.1017/s1431927620021881","intvolume":"        26","publication_identifier":{"eissn":["1435-8115"],"issn":["1431-9276"]},"page":"2518-2519","_id":"15286","day":"01","publication":"Microscopy and Microanalysis","quality_controlled":"1","title":"Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration","issue":"S2"},{"quality_controlled":"1","title":"Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"intvolume":"        11","status":"public","language":[{"iso":"eng"}],"author":[{"id":"404F5528-F248-11E8-B48F-1D18A9856A87","first_name":"Florian","full_name":"Fäßler, Florian","last_name":"Fäßler","orcid":"0000-0001-7149-769X"},{"orcid":"0000-0001-8370-6161","last_name":"Dimchev","first_name":"Georgi A","full_name":"Dimchev, Georgi A","id":"38C393BE-F248-11E8-B48F-1D18A9856A87"},{"id":"3661B498-F248-11E8-B48F-1D18A9856A87","full_name":"Hodirnau, Victor-Valentin","first_name":"Victor-Valentin","orcid":"0000-0003-3904-947X","last_name":"Hodirnau"},{"first_name":"William","full_name":"Wan, William","last_name":"Wan"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur","orcid":"0000-0003-4790-8078","first_name":"Florian KM","full_name":"Schur, Florian KM"}],"external_id":{"isi":["000603078000003"]},"corr_author":"1","article_type":"original","date_created":"2020-12-23T08:25:45Z","ddc":["570"],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_number":"6437","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"volume":11,"related_material":{"link":[{"url":"https://ist.ac.at/en/news/cutting-edge-technology-reveals-structures-within-cells/","relation":"press_release","description":"News on IST Homepage"}]},"has_accepted_license":"1","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"Bio"},{"_id":"EM-Fac"}],"file_date_updated":"2020-12-28T08:16:10Z","publication":"Nature Communications","day":"22","_id":"8971","doi":"10.1038/s41467-020-20286-x","publication_identifier":{"issn":["2041-1723"]},"acknowledgement":"This research was supported by the Scientific Service Units (SSUs) of IST Austria through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), the BioImaging Facility (BIF), and the Electron Microscopy Facility (EMF). We also thank Dimitry Tegunov (MPI for Biophysical Chemistry) for helpful discussions\r\nabout the M software, and Michael Sixt (IST Austria) and Klemens Rottner (Technical University Braunschweig, HZI Braunschweig) for critical reading of the manuscript. We also thank Gregory Voth (University of Chicago) for providing us the MD-derived branch junction model for comparison. The authors acknowledge support from IST Austria and from the Austrian Science Fund (FWF): M02495 to G.D. and Austrian Science Fund (FWF): P33367 to F.K.M.S. ","oa":1,"type":"journal_article","department":[{"_id":"FlSc"},{"_id":"EM-Fac"}],"citation":{"ieee":"F. Fäßler, G. A. Dimchev, V.-V. Hodirnau, W. Wan, and F. K. Schur, “Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction,” <i>Nature Communications</i>, vol. 11. Springer Nature, 2020.","chicago":"Fäßler, Florian, Georgi A Dimchev, Victor-Valentin Hodirnau, William Wan, and Florian KM Schur. “Cryo-Electron Tomography Structure of Arp2/3 Complex in Cells Reveals New Insights into the Branch Junction.” <i>Nature Communications</i>. Springer Nature, 2020. <a href=\"https://doi.org/10.1038/s41467-020-20286-x\">https://doi.org/10.1038/s41467-020-20286-x</a>.","ama":"Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction. <i>Nature Communications</i>. 2020;11. doi:<a href=\"https://doi.org/10.1038/s41467-020-20286-x\">10.1038/s41467-020-20286-x</a>","mla":"Fäßler, Florian, et al. “Cryo-Electron Tomography Structure of Arp2/3 Complex in Cells Reveals New Insights into the Branch Junction.” <i>Nature Communications</i>, vol. 11, 6437, Springer Nature, 2020, doi:<a href=\"https://doi.org/10.1038/s41467-020-20286-x\">10.1038/s41467-020-20286-x</a>.","short":"F. Fäßler, G.A. Dimchev, V.-V. Hodirnau, W. Wan, F.K. Schur, Nature Communications 11 (2020).","ista":"Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. 2020. Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction. Nature Communications. 11, 6437.","apa":"Fäßler, F., Dimchev, G. A., Hodirnau, V.-V., Wan, W., &#38; Schur, F. K. (2020). Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-020-20286-x\">https://doi.org/10.1038/s41467-020-20286-x</a>"},"publication_status":"published","article_processing_charge":"No","project":[{"grant_number":"P33367","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","name":"Structure and isoform diversity of the Arp2/3 complex"},{"grant_number":"M02495","call_identifier":"FWF","name":"Protein structure and function in filopodia across scales","_id":"2674F658-B435-11E9-9278-68D0E5697425"}],"oa_version":"Published Version","file":[{"content_type":"application/pdf","checksum":"55d43ea0061cc4027ba45e966e1db8cc","file_name":"2020_NatureComm_Faessler.pdf","file_size":3958727,"date_updated":"2020-12-28T08:16:10Z","success":1,"file_id":"8975","creator":"dernst","access_level":"open_access","relation":"main_file","date_created":"2020-12-28T08:16:10Z"}],"abstract":[{"text":"The actin-related protein (Arp)2/3 complex nucleates branched actin filament networks pivotal for cell migration, endocytosis and pathogen infection. Its activation is tightly regulated and involves complex structural rearrangements and actin filament binding, which are yet to be understood. Here, we report a 9.0 Å resolution structure of the actin filament Arp2/3 complex branch junction in cells using cryo-electron tomography and subtomogram averaging. This allows us to generate an accurate model of the active Arp2/3 complex in the branch junction and its interaction with actin filaments. Notably, our model reveals a previously undescribed set of interactions of the Arp2/3 complex with the mother filament, significantly different to the previous branch junction model. Our structure also indicates a central role for the ArpC3 subunit in stabilizing the active conformation.","lang":"eng"}],"scopus_import":"1","year":"2020","date_updated":"2025-04-15T07:52:12Z","isi":1,"month":"12","date_published":"2020-12-22T00:00:00Z","publisher":"Springer Nature"},{"language":[{"iso":"eng"}],"external_id":{"pmid":["31986188"],"isi":["000510746400010"]},"author":[{"last_name":"Dick","first_name":"Robert A.","full_name":"Dick, Robert A."},{"last_name":"Xu","full_name":"Xu, Chaoyi","first_name":"Chaoyi"},{"last_name":"Morado","first_name":"Dustin R.","full_name":"Morado, Dustin R."},{"id":"4D62F2A6-F248-11E8-B48F-1D18A9856A87","first_name":"Vladyslav","full_name":"Kravchuk, Vladyslav","orcid":"0000-0001-9523-9089","last_name":"Kravchuk"},{"first_name":"Clifton L.","full_name":"Ricana, Clifton L.","last_name":"Ricana"},{"full_name":"Lyddon, Terri D.","first_name":"Terri D.","last_name":"Lyddon"},{"last_name":"Broad","first_name":"Arianna M.","full_name":"Broad, Arianna M."},{"first_name":"J. Ryan","full_name":"Feathers, J. Ryan","last_name":"Feathers"},{"last_name":"Johnson","first_name":"Marc C.","full_name":"Johnson, Marc C."},{"last_name":"Vogt","full_name":"Vogt, Volker M.","first_name":"Volker M."},{"last_name":"Perilla","full_name":"Perilla, Juan R.","first_name":"Juan R."},{"first_name":"John A. G.","full_name":"Briggs, John A. G.","last_name":"Briggs"},{"last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","first_name":"Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}],"intvolume":"        16","status":"public","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"quality_controlled":"1","title":"Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly","has_accepted_license":"1","volume":16,"related_material":{"record":[{"relation":"research_data","status":"deleted","id":"9723"}]},"article_number":"e1008277","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"corr_author":"1","article_type":"original","date_created":"2020-02-06T18:47:17Z","ddc":["570"],"oa":1,"citation":{"ista":"Dick RA, Xu C, Morado DR, Kravchuk V, Ricana CL, Lyddon TD, Broad AM, Feathers JR, Johnson MC, Vogt VM, Perilla JR, Briggs JAG, Schur FK. 2020. Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly. PLOS Pathogens. 16(1), e1008277.","apa":"Dick, R. A., Xu, C., Morado, D. R., Kravchuk, V., Ricana, C. L., Lyddon, T. D., … Schur, F. K. (2020). Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly. <i>PLOS Pathogens</i>. Public Library of Science. <a href=\"https://doi.org/10.1371/journal.ppat.1008277\">https://doi.org/10.1371/journal.ppat.1008277</a>","mla":"Dick, Robert A., et al. “Structures of Immature EIAV Gag Lattices Reveal a Conserved Role for IP6 in Lentivirus Assembly.” <i>PLOS Pathogens</i>, vol. 16, no. 1, e1008277, Public Library of Science, 2020, doi:<a href=\"https://doi.org/10.1371/journal.ppat.1008277\">10.1371/journal.ppat.1008277</a>.","ama":"Dick RA, Xu C, Morado DR, et al. Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly. <i>PLOS Pathogens</i>. 2020;16(1). doi:<a href=\"https://doi.org/10.1371/journal.ppat.1008277\">10.1371/journal.ppat.1008277</a>","short":"R.A. Dick, C. Xu, D.R. Morado, V. Kravchuk, C.L. Ricana, T.D. Lyddon, A.M. Broad, J.R. Feathers, M.C. Johnson, V.M. Vogt, J.R. Perilla, J.A.G. Briggs, F.K. Schur, PLOS Pathogens 16 (2020).","chicago":"Dick, Robert A., Chaoyi Xu, Dustin R. Morado, Vladyslav Kravchuk, Clifton L. Ricana, Terri D. Lyddon, Arianna M. Broad, et al. “Structures of Immature EIAV Gag Lattices Reveal a Conserved Role for IP6 in Lentivirus Assembly.” <i>PLOS Pathogens</i>. Public Library of Science, 2020. <a href=\"https://doi.org/10.1371/journal.ppat.1008277\">https://doi.org/10.1371/journal.ppat.1008277</a>.","ieee":"R. A. Dick <i>et al.</i>, “Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly,” <i>PLOS Pathogens</i>, vol. 16, no. 1. Public Library of Science, 2020."},"type":"journal_article","department":[{"_id":"FlSc"}],"doi":"10.1371/journal.ppat.1008277","publication_identifier":{"issn":["1553-7374"]},"_id":"7464","day":"27","file_date_updated":"2020-07-14T12:47:59Z","acknowledged_ssus":[{"_id":"ScienComp"}],"issue":"1","publication":"PLOS Pathogens","date_published":"2020-01-27T00:00:00Z","publisher":"Public Library of Science","scopus_import":"1","year":"2020","abstract":[{"lang":"eng","text":"Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, trimeric, and hexameric protein contacts. Among retroviruses the inter- and intra-hexamer contacts differ, especially in the N-terminal sub-domain of CA (CANTD). For HIV-1 the cellular molecule inositol hexakisphosphate (IP6) interacts with and stabilizes the immature hexamer, and is required for production of infectious virus particles. We have used in vitro assembly, cryo-electron tomography and subtomogram averaging, atomistic molecular dynamics simulations and mutational analyses to study the HIV-related lentivirus equine infectious anemia virus (EIAV). In particular, we sought to understand the structural conservation of the immature lentivirus lattice and the role of IP6 in EIAV assembly. Similar to HIV-1, IP6 strongly promoted in vitro assembly of EIAV Gag proteins into virus-like particles (VLPs), which took three morphologically highly distinct forms: narrow tubes, wide tubes, and spheres. Structural characterization of these VLPs to sub-4Å resolution unexpectedly showed that all three morphologies are based on an immature lattice with preserved key structural components, highlighting the structural versatility of CA to form immature assemblies. A direct comparison between EIAV and HIV revealed that both lentiviruses maintain similar immature interfaces, which are established by both conserved and non-conserved residues. In both EIAV and HIV-1, IP6 regulates immature assembly via conserved lysine residues within the CACTD and SP. Lastly, we demonstrate that IP6 stimulates in vitro assembly of immature particles of several other retroviruses in the lentivirus genus, suggesting a conserved role for IP6 in lentiviral assembly."}],"date_updated":"2025-04-15T08:24:51Z","isi":1,"month":"01","oa_version":"Published Version","file":[{"file_id":"7484","creator":"dernst","access_level":"open_access","relation":"main_file","date_created":"2020-02-11T10:07:28Z","content_type":"application/pdf","checksum":"a297f54d1fef0efe4789ca00f37f241e","file_name":"2020_PLOSPatho_Dick.pdf","file_size":4551246,"date_updated":"2020-07-14T12:47:59Z"}],"publication_status":"published","article_processing_charge":"No","project":[{"_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid","call_identifier":"FWF","grant_number":"P31445"}]},{"status":"public","intvolume":"        11","external_id":{"pmid":["32054835"],"isi":["000514928000017"]},"author":[{"last_name":"Turoňová","full_name":"Turoňová, Beata","first_name":"Beata"},{"last_name":"Hagen","first_name":"Wim J.H.","full_name":"Hagen, Wim J.H."},{"id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","full_name":"Obr, Martin","first_name":"Martin","orcid":"0000-0003-1756-6564","last_name":"Obr"},{"last_name":"Mosalaganti","first_name":"Shyamal","full_name":"Mosalaganti, Shyamal"},{"last_name":"Beugelink","first_name":"J. Wouter","full_name":"Beugelink, J. Wouter"},{"last_name":"Zimmerli","full_name":"Zimmerli, Christian E.","first_name":"Christian E."},{"last_name":"Kräusslich","full_name":"Kräusslich, Hans Georg","first_name":"Hans Georg"},{"first_name":"Martin","full_name":"Beck, Martin","last_name":"Beck"}],"language":[{"iso":"eng"}],"title":"Benchmarking tomographic acquisition schemes for high-resolution structural biology","quality_controlled":"1","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"volume":11,"has_accepted_license":"1","ddc":["570"],"date_created":"2020-02-23T23:00:35Z","article_type":"original","pmid":1,"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","article_number":"876","publication_identifier":{"eissn":["2041-1723"]},"doi":"10.1038/s41467-020-14535-2","department":[{"_id":"FlSc"}],"citation":{"chicago":"Turoňová, Beata, Wim J.H. Hagen, Martin Obr, Shyamal Mosalaganti, J. Wouter Beugelink, Christian E. Zimmerli, Hans Georg Kräusslich, and Martin Beck. “Benchmarking Tomographic Acquisition Schemes for High-Resolution Structural Biology.” <i>Nature Communications</i>. Springer Nature, 2020. <a href=\"https://doi.org/10.1038/s41467-020-14535-2\">https://doi.org/10.1038/s41467-020-14535-2</a>.","ieee":"B. Turoňová <i>et al.</i>, “Benchmarking tomographic acquisition schemes for high-resolution structural biology,” <i>Nature Communications</i>, vol. 11. Springer Nature, 2020.","apa":"Turoňová, B., Hagen, W. J. H., Obr, M., Mosalaganti, S., Beugelink, J. W., Zimmerli, C. E., … Beck, M. (2020). Benchmarking tomographic acquisition schemes for high-resolution structural biology. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-020-14535-2\">https://doi.org/10.1038/s41467-020-14535-2</a>","ista":"Turoňová B, Hagen WJH, Obr M, Mosalaganti S, Beugelink JW, Zimmerli CE, Kräusslich HG, Beck M. 2020. Benchmarking tomographic acquisition schemes for high-resolution structural biology. Nature Communications. 11, 876.","short":"B. Turoňová, W.J.H. Hagen, M. Obr, S. Mosalaganti, J.W. Beugelink, C.E. Zimmerli, H.G. Kräusslich, M. Beck, Nature Communications 11 (2020).","ama":"Turoňová B, Hagen WJH, Obr M, et al. Benchmarking tomographic acquisition schemes for high-resolution structural biology. <i>Nature Communications</i>. 2020;11. doi:<a href=\"https://doi.org/10.1038/s41467-020-14535-2\">10.1038/s41467-020-14535-2</a>","mla":"Turoňová, Beata, et al. “Benchmarking Tomographic Acquisition Schemes for High-Resolution Structural Biology.” <i>Nature Communications</i>, vol. 11, 876, Springer Nature, 2020, doi:<a href=\"https://doi.org/10.1038/s41467-020-14535-2\">10.1038/s41467-020-14535-2</a>."},"type":"journal_article","oa":1,"publication":"Nature Communications","file_date_updated":"2020-07-14T12:47:59Z","day":"13","_id":"7511","isi":1,"month":"02","date_updated":"2026-04-03T09:27:26Z","scopus_import":"1","year":"2020","abstract":[{"text":"Cryo electron tomography with subsequent subtomogram averaging is a powerful technique to structurally analyze macromolecular complexes in their native context. Although close to atomic resolution in principle can be obtained, it is not clear how individual experimental parameters contribute to the attainable resolution. Here, we have used immature HIV-1 lattice as a benchmarking sample to optimize the attainable resolution for subtomogram averaging. We systematically tested various experimental parameters such as the order of projections, different angular increments and the use of the Volta phase plate. We find that although any of the prominently used acquisition schemes is sufficient to obtain subnanometer resolution, dose-symmetric acquisition provides considerably better outcome. We discuss our findings in order to provide guidance for data acquisition. Our data is publicly available and might be used to further develop processing routines.","lang":"eng"}],"publisher":"Springer Nature","date_published":"2020-02-13T00:00:00Z","article_processing_charge":"No","publication_status":"published","oa_version":"Published Version","file":[{"file_id":"7517","date_created":"2020-02-24T14:00:54Z","relation":"main_file","access_level":"open_access","creator":"dernst","file_name":"2020_NatureComm_Turonova.pdf","checksum":"2c8d10475e1b0d397500760e28bdf561","content_type":"application/pdf","date_updated":"2020-07-14T12:47:59Z","file_size":2027529}]},{"publication_status":"published","article_processing_charge":"Yes (via OA deal)","project":[{"grant_number":"P33367","name":"Structure and isoform diversity of the Arp2/3 complex","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A"},{"name":"NÖ-Fonds Preis für die Jungforscherin des Jahres am IST Austria","_id":"059B463C-7A3F-11EA-A408-12923DDC885E"}],"file":[{"date_created":"2020-12-10T14:01:10Z","relation":"main_file","access_level":"open_access","creator":"dernst","file_id":"8937","success":1,"date_updated":"2020-12-10T14:01:10Z","file_size":7076870,"file_name":"2020_JourStrucBiology_Faessler.pdf","checksum":"c48cbf594e84fc2f91966ffaafc0918c","content_type":"application/pdf"}],"oa_version":"Published Version","abstract":[{"lang":"eng","text":"Cryo-electron microscopy (cryo-EM) of cellular specimens provides insights into biological processes and structures within a native context. However, a major challenge still lies in the efficient and reproducible preparation of adherent cells for subsequent cryo-EM analysis. This is due to the sensitivity of many cellular specimens to the varying seeding and culturing conditions required for EM experiments, the often limited amount of cellular material and also the fragility of EM grids and their substrate. Here, we present low-cost and reusable 3D printed grid holders, designed to improve specimen preparation when culturing challenging cellular samples directly on grids. The described grid holders increase cell culture reproducibility and throughput, and reduce the resources required for cell culturing. We show that grid holders can be integrated into various cryo-EM workflows, including micro-patterning approaches to control cell seeding on grids, and for generating samples for cryo-focused ion beam milling and cryo-electron tomography experiments. Their adaptable design allows for the generation of specialized grid holders customized to a large variety of applications."}],"year":"2020","scopus_import":"1","date_updated":"2026-06-16T22:30:09Z","isi":1,"month":"12","date_published":"2020-12-01T00:00:00Z","publisher":"Elsevier","file_date_updated":"2020-12-10T14:01:10Z","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"Bio"},{"_id":"EM-Fac"}],"issue":"3","publication":"Journal of Structural Biology","_id":"8586","day":"01","doi":"10.1016/j.jsb.2020.107633","publication_identifier":{"issn":["1047-8477"]},"acknowledgement":"This work was supported by the Austrian Science Fund (FWF, P33367) to FKMS. BZ acknowledges support by the Niederösterreich Fond. This research was also supported by the Scientific Service Units (SSU) of IST Austria through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), the BioImaging Facility (BIF) and the Electron Microscopy Facility (EMF). We thank Georgi Dimchev (IST Austria) and Sonja Jacob (Vienna Biocenter Core Facilities) for testing our grid holders in different experimental setups and Daniel Gütl and the Kondrashov group (IST Austria) for granting us repeated access to their 3D printers. We also thank Jonna Alanko and the Sixt lab (IST Austria) for providing us HeLa cells, primary BL6 mouse tail fibroblasts, NIH 3T3 fibroblasts and human telomerase immortalised foreskin fibroblasts for our experiments. We are thankful to Ori Avinoam and William Wan for helpful comments on the manuscript and also thank Dorotea Fracchiolla (Art&Science) for illustrating the graphical abstract.","oa":1,"department":[{"_id":"FlSc"}],"citation":{"short":"F. Fäßler, B. Zens, R. Hauschild, F.K. Schur, Journal of Structural Biology 212 (2020).","mla":"Fäßler, Florian, et al. “3D Printed Cell Culture Grid Holders for Improved Cellular Specimen Preparation in Cryo-Electron Microscopy.” <i>Journal of Structural Biology</i>, vol. 212, no. 3, 107633, Elsevier, 2020, doi:<a href=\"https://doi.org/10.1016/j.jsb.2020.107633\">10.1016/j.jsb.2020.107633</a>.","ama":"Fäßler F, Zens B, Hauschild R, Schur FK. 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy. <i>Journal of Structural Biology</i>. 2020;212(3). doi:<a href=\"https://doi.org/10.1016/j.jsb.2020.107633\">10.1016/j.jsb.2020.107633</a>","ista":"Fäßler F, Zens B, Hauschild R, Schur FK. 2020. 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy. Journal of Structural Biology. 212(3), 107633.","apa":"Fäßler, F., Zens, B., Hauschild, R., &#38; Schur, F. K. (2020). 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy. <i>Journal of Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jsb.2020.107633\">https://doi.org/10.1016/j.jsb.2020.107633</a>","ieee":"F. Fäßler, B. Zens, R. Hauschild, and F. K. Schur, “3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy,” <i>Journal of Structural Biology</i>, vol. 212, no. 3. Elsevier, 2020.","chicago":"Fäßler, Florian, Bettina Zens, Robert Hauschild, and Florian KM Schur. “3D Printed Cell Culture Grid Holders for Improved Cellular Specimen Preparation in Cryo-Electron Microscopy.” <i>Journal of Structural Biology</i>. Elsevier, 2020. <a href=\"https://doi.org/10.1016/j.jsb.2020.107633\">https://doi.org/10.1016/j.jsb.2020.107633</a>."},"type":"journal_article","corr_author":"1","article_type":"original","date_created":"2020-09-29T13:24:06Z","ddc":["570"],"article_number":"107633","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["electron microscopy","cryo-EM","EM sample preparation","3D printing","cell culture"],"pmid":1,"volume":212,"related_material":{"record":[{"relation":"used_in_publication","status":"public","id":"14592"},{"relation":"dissertation_contains","status":"public","id":"12491"}]},"has_accepted_license":"1","quality_controlled":"1","title":"3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"intvolume":"       212","status":"public","language":[{"iso":"eng"}],"external_id":{"pmid":["32987119"],"isi":["000600997800008"]},"author":[{"full_name":"Fäßler, Florian","first_name":"Florian","orcid":"0000-0001-7149-769X","last_name":"Fäßler","id":"404F5528-F248-11E8-B48F-1D18A9856A87"},{"id":"45FD126C-F248-11E8-B48F-1D18A9856A87","last_name":"Zens","orcid":"0000-0002-9561-1239","first_name":"Bettina","full_name":"Zens, Bettina"},{"last_name":"Hauschild","orcid":"0000-0001-9843-3522","first_name":"Robert","full_name":"Hauschild, Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0003-4790-8078","last_name":"Schur","first_name":"Florian KM","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}]},{"day":"09","_id":"8434","publication":"Journal of Cell Science","issue":"7","file_date_updated":"2020-10-11T22:30:02Z","department":[{"_id":"FlSc"}],"type":"journal_article","citation":{"short":"G.A. Dimchev, B. Amiri, A.C. Humphries, M. Schaks, V. Dimchev, T.E.B. Stradal, J. Faix, M. Krause, M. Way, M. Falcke, K. Rottner, Journal of Cell Science 133 (2020).","mla":"Dimchev, Georgi A., et al. “Lamellipodin Tunes Cell Migration by Stabilizing Protrusions and Promoting Adhesion Formation.” <i>Journal of Cell Science</i>, vol. 133, no. 7, jcs239020, The Company of Biologists, 2020, doi:<a href=\"https://doi.org/10.1242/jcs.239020\">10.1242/jcs.239020</a>.","ama":"Dimchev GA, Amiri B, Humphries AC, et al. Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. <i>Journal of Cell Science</i>. 2020;133(7). doi:<a href=\"https://doi.org/10.1242/jcs.239020\">10.1242/jcs.239020</a>","ista":"Dimchev GA, Amiri B, Humphries AC, Schaks M, Dimchev V, Stradal TEB, Faix J, Krause M, Way M, Falcke M, Rottner K. 2020. Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. Journal of Cell Science. 133(7), jcs239020.","apa":"Dimchev, G. A., Amiri, B., Humphries, A. C., Schaks, M., Dimchev, V., Stradal, T. E. B., … Rottner, K. (2020). Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation. <i>Journal of Cell Science</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.239020\">https://doi.org/10.1242/jcs.239020</a>","ieee":"G. A. Dimchev <i>et al.</i>, “Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation,” <i>Journal of Cell Science</i>, vol. 133, no. 7. The Company of Biologists, 2020.","chicago":"Dimchev, Georgi A, Behnam Amiri, Ashley C. Humphries, Matthias Schaks, Vanessa Dimchev, Theresia E. B. Stradal, Jan Faix, et al. “Lamellipodin Tunes Cell Migration by Stabilizing Protrusions and Promoting Adhesion Formation.” <i>Journal of Cell Science</i>. The Company of Biologists, 2020. <a href=\"https://doi.org/10.1242/jcs.239020\">https://doi.org/10.1242/jcs.239020</a>."},"oa":1,"publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"acknowledgement":"This work was supported in part by Deutsche Forschungsgemeinschaft (DFG)[GRK2223/1, RO2414/5-1 (to K.R.), FA350/11-1 (to M.F.) and FA330/11-1 (to J.F.)],as well as by intramural funding from the Helmholtz Association (to T.E.B.S. andK.R.). G.D. was additionally funded by the Austrian Science Fund (FWF) LiseMeitner Program [M-2495]. A.C.H. and M.W. are supported by the Francis CrickInstitute, which receives its core funding from Cancer Research UK [FC001209], theMedical Research Council [FC001209] and the Wellcome Trust [FC001209]. M.K. issupported by the Biotechnology and Biological Sciences Research Council [BB/F011431/1, BB/J000590/1, BB/N000226/1]. Deposited in PMC for release after 6months.","doi":"10.1242/jcs.239020","file":[{"date_created":"2020-09-17T14:07:51Z","relation":"main_file","access_level":"open_access","creator":"dernst","embargo":"2020-10-10","file_id":"8435","date_updated":"2020-10-11T22:30:02Z","file_size":13493302,"file_name":"2020_JournalCellScience_Dimchev.pdf","checksum":"ba917e551acc4ece2884b751434df9ae","content_type":"application/pdf"}],"oa_version":"Published Version","project":[{"grant_number":"M02495","call_identifier":"FWF","name":"Protein structure and function in filopodia across scales","_id":"2674F658-B435-11E9-9278-68D0E5697425"}],"article_processing_charge":"No","publication_status":"published","publisher":"The Company of Biologists","date_published":"2020-04-09T00:00:00Z","month":"04","isi":1,"date_updated":"2025-04-15T07:52:13Z","year":"2020","scopus_import":"1","abstract":[{"text":"Efficient migration on adhesive surfaces involves the protrusion of lamellipodial actin networks and their subsequent stabilization by nascent adhesions. The actin-binding protein lamellipodin (Lpd) is thought to play a critical role in lamellipodium protrusion, by delivering Ena/VASP proteins onto the growing plus ends of actin filaments and by interacting with the WAVE regulatory complex, an activator of the Arp2/3 complex, at the leading edge. Using B16-F1 melanoma cell lines, we demonstrate that genetic ablation of Lpd compromises protrusion efficiency and coincident cell migration without altering essential parameters of lamellipodia, including their maximal rate of forward advancement and actin polymerization. We also confirmed lamellipodia and migration phenotypes with CRISPR/Cas9-mediated Lpd knockout Rat2 fibroblasts, excluding cell type-specific effects. Moreover, computer-aided analysis of cell-edge morphodynamics on B16-F1 cell lamellipodia revealed that loss of Lpd correlates with reduced temporal protrusion maintenance as a prerequisite of nascent adhesion formation. We conclude that Lpd optimizes protrusion and nascent adhesion formation by counteracting frequent, chaotic retraction and membrane ruffling.This article has an associated First Person interview with the first author of the paper. ","lang":"eng"}],"title":"Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation","quality_controlled":"1","external_id":{"isi":["000534387800005"],"pmid":[" 32094266"]},"author":[{"orcid":"0000-0001-8370-6161","last_name":"Dimchev","first_name":"Georgi A","full_name":"Dimchev, Georgi A","id":"38C393BE-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Amiri, Behnam","first_name":"Behnam","last_name":"Amiri"},{"full_name":"Humphries, Ashley C.","first_name":"Ashley C.","last_name":"Humphries"},{"first_name":"Matthias","full_name":"Schaks, Matthias","last_name":"Schaks"},{"first_name":"Vanessa","full_name":"Dimchev, Vanessa","last_name":"Dimchev"},{"first_name":"Theresia E. B.","full_name":"Stradal, Theresia E. B.","last_name":"Stradal"},{"full_name":"Faix, Jan","first_name":"Jan","last_name":"Faix"},{"last_name":"Krause","full_name":"Krause, Matthias","first_name":"Matthias"},{"last_name":"Way","full_name":"Way, Michael","first_name":"Michael"},{"last_name":"Falcke","first_name":"Martin","full_name":"Falcke, Martin"},{"last_name":"Rottner","first_name":"Klemens","full_name":"Rottner, Klemens"}],"language":[{"iso":"eng"}],"status":"public","intvolume":"       133","pmid":1,"keyword":["Cell Biology"],"article_number":"jcs239020","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","ddc":["570"],"date_created":"2020-09-17T14:00:33Z","article_type":"original","has_accepted_license":"1","volume":133},{"publisher":"Nature Publishing Group","date_published":"2019-01-23T00:00:00Z","year":"2019","abstract":[{"text":"Microalgae of the genus Chlorella vulgaris are candidates for the production of lipids for biofuel production. Besides that, Chlorella vulgaris is marketed as protein and vitamin rich food additive. Its potential as a novel expression system for recombinant proteins inspired us to study its asparagine-linked oligosaccharides (N-glycans) by mass spectrometry, chromatography and gas chromatography. Oligomannosidic N-glycans with up to nine mannoses were the structures found in culture collection strains as well as several commercial products. These glycans co-eluted with plant N-glycans in the highly shape selective porous graphitic carbon chromatography. Thus, Chlorella vulgaris generates oligomannosidic N-glycans of the structural type known from land plants and animals. In fact, Man5 (Man5GlcNAc2) served as substrate for GlcNAc-transferase I and a trace of an endogenous structure with terminal GlcNAc was seen. The unusual more linear Man5 structure recently found on glycoproteins of Chlamydomonas reinhardtii occurred - if at all - in traces only. Notably, a majority of the oligomannosidic glycans was multiply O-methylated with 3-O-methyl and 3,6-di-O-methyl mannoses at the non-reducing termini. This modification has so far been neither found on plant nor vertebrate N-glycans. It’s possible immunogenicity raises concerns as to the use of C. vulgaris for production of pharmaceutical glycoproteins.","lang":"eng"}],"scopus_import":"1","month":"01","isi":1,"date_updated":"2023-08-24T14:33:16Z","file":[{"file_size":2124292,"date_updated":"2020-07-14T12:47:13Z","content_type":"application/pdf","checksum":"4129c7d7663d1f8a1edf8c4232372f66","file_name":"2019_ScientificReports_Mocsai.pdf","creator":"dernst","access_level":"open_access","relation":"main_file","date_created":"2019-02-05T13:10:02Z","file_id":"5923"}],"oa_version":"Published Version","publication_status":"published","article_processing_charge":"No","oa":1,"citation":{"apa":"Mócsai, R., Figl, R., Troschl, C., Strasser, R., Svehla, E., Windwarder, M., … Altmann, F. (2019). N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated. <i>Scientific Reports</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/s41598-018-36884-1\">https://doi.org/10.1038/s41598-018-36884-1</a>","ista":"Mócsai R, Figl R, Troschl C, Strasser R, Svehla E, Windwarder M, Thader A, Altmann F. 2019. N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated. Scientific Reports. 9(1), 331.","mla":"Mócsai, Réka, et al. “N-Glycans of the Microalga Chlorella Vulgaris Are of the Oligomannosidic Type but Highly Methylated.” <i>Scientific Reports</i>, vol. 9, no. 1, 331, Nature Publishing Group, 2019, doi:<a href=\"https://doi.org/10.1038/s41598-018-36884-1\">10.1038/s41598-018-36884-1</a>.","ama":"Mócsai R, Figl R, Troschl C, et al. N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated. <i>Scientific Reports</i>. 2019;9(1). doi:<a href=\"https://doi.org/10.1038/s41598-018-36884-1\">10.1038/s41598-018-36884-1</a>","short":"R. Mócsai, R. Figl, C. Troschl, R. Strasser, E. Svehla, M. Windwarder, A. Thader, F. Altmann, Scientific Reports 9 (2019).","chicago":"Mócsai, Réka, Rudolf Figl, Clemens Troschl, Richard Strasser, Elisabeth Svehla, Markus Windwarder, Andreas Thader, and Friedrich Altmann. “N-Glycans of the Microalga Chlorella Vulgaris Are of the Oligomannosidic Type but Highly Methylated.” <i>Scientific Reports</i>. Nature Publishing Group, 2019. <a href=\"https://doi.org/10.1038/s41598-018-36884-1\">https://doi.org/10.1038/s41598-018-36884-1</a>.","ieee":"R. Mócsai <i>et al.</i>, “N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated,” <i>Scientific Reports</i>, vol. 9, no. 1. Nature Publishing Group, 2019."},"department":[{"_id":"FlSc"}],"type":"journal_article","doi":"10.1038/s41598-018-36884-1","day":"23","_id":"5907","issue":"1","file_date_updated":"2020-07-14T12:47:13Z","publication":"Scientific Reports","has_accepted_license":"1","volume":9,"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_number":"331","ddc":["580"],"date_created":"2019-02-03T22:59:13Z","author":[{"first_name":"Réka","full_name":"Mócsai, Réka","last_name":"Mócsai"},{"full_name":"Figl, Rudolf","first_name":"Rudolf","last_name":"Figl"},{"last_name":"Troschl","first_name":"Clemens","full_name":"Troschl, Clemens"},{"last_name":"Strasser","full_name":"Strasser, Richard","first_name":"Richard"},{"last_name":"Svehla","full_name":"Svehla, Elisabeth","first_name":"Elisabeth"},{"first_name":"Markus","full_name":"Windwarder, Markus","last_name":"Windwarder"},{"id":"3A18A7B8-F248-11E8-B48F-1D18A9856A87","last_name":"Thader","full_name":"Thader, Andreas","first_name":"Andreas"},{"first_name":"Friedrich","full_name":"Altmann, Friedrich","last_name":"Altmann"}],"external_id":{"isi":["000456392400012"]},"language":[{"iso":"eng"}],"intvolume":"         9","status":"public","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"title":"N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated","quality_controlled":"1"},{"date_published":"2019-10-01T00:00:00Z","publisher":"Elsevier","date_updated":"2023-08-25T10:13:31Z","isi":1,"month":"10","scopus_import":"1","year":"2019","abstract":[{"lang":"eng","text":"Cryo-electron tomography (cryo-ET) provides unprecedented insights into the molecular constituents of biological environments. In combination with an image processing method called subtomogram averaging (STA), detailed 3D structures of biological molecules can be obtained in large, irregular macromolecular assemblies or in situ, without the need for purification. The contextual meta-information these methods also provide, such as a protein’s location within its native environment, can then be combined with functional data. This allows the derivation of a detailed view on the physiological or pathological roles of proteins from the molecular to cellular level. Despite their tremendous potential in in situ structural biology, cryo-ET and STA have been restricted by methodological limitations, such as the low obtainable resolution. Exciting progress now allows one to reach unprecedented resolutions in situ, ranging in optimal cases beyond the nanometer barrier. Here, I review current frontiers and future challenges in routinely determining high-resolution structures in in situ environments using cryo-ET and STA."}],"oa_version":"None","article_processing_charge":"No","publication_status":"published","citation":{"apa":"Schur, F. K. (2019). Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">https://doi.org/10.1016/j.sbi.2019.03.018</a>","ista":"Schur FK. 2019. Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. Current Opinion in Structural Biology. 58(10), 1–9.","short":"F.K. Schur, Current Opinion in Structural Biology 58 (2019) 1–9.","ama":"Schur FK. Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. <i>Current Opinion in Structural Biology</i>. 2019;58(10):1-9. doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">10.1016/j.sbi.2019.03.018</a>","mla":"Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural Biology</i>, vol. 58, no. 10, Elsevier, 2019, pp. 1–9, doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">10.1016/j.sbi.2019.03.018</a>.","chicago":"Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">https://doi.org/10.1016/j.sbi.2019.03.018</a>.","ieee":"F. K. Schur, “Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging,” <i>Current Opinion in Structural Biology</i>, vol. 58, no. 10. Elsevier, pp. 1–9, 2019."},"department":[{"_id":"FlSc"}],"type":"journal_article","doi":"10.1016/j.sbi.2019.03.018","acknowledgement":"The author acknowledges support from IST Austria and the Austrian Science Fund (FWF).","publication_identifier":{"issn":["0959-440X"]},"day":"01","_id":"6343","publication":"Current Opinion in Structural Biology","issue":"10","volume":58,"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","date_created":"2019-04-19T11:19:13Z","article_type":"original","language":[{"iso":"eng"}],"external_id":{"isi":["000494891800004"]},"author":[{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur","orcid":"0000-0003-4790-8078"}],"status":"public","intvolume":"        58","page":"1-9","quality_controlled":"1","title":"Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging"},{"quality_controlled":"1","title":"Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging","page":"117-159","intvolume":"       105","status":"public","language":[{"iso":"eng"}],"external_id":{"isi":["000501594500006"],"pmid":["    31522703"]},"author":[{"id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","full_name":"Obr, Martin","orcid":"0000-0003-1756-6564","last_name":"Obr"},{"full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur","orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}],"date_created":"2019-09-18T08:15:37Z","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","pmid":1,"volume":105,"publication":"Complementary Strategies to Study Virus Structure and Function","editor":[{"first_name":"Félix A.","full_name":"Rey, Félix A.","last_name":"Rey"}],"_id":"6890","day":"27","doi":"10.1016/bs.aivir.2019.07.008","publication_identifier":{"issn":["0065-3527"],"isbn":["9780128184561"]},"type":"book_chapter","citation":{"chicago":"Obr, Martin, and Florian KM Schur. “Structural Analysis of Pleomorphic and Asymmetric Viruses Using Cryo-Electron Tomography and Subtomogram Averaging.” In <i>Complementary Strategies to Study Virus Structure and Function</i>, edited by Félix A. Rey, 105:117–59. Advances in Virus Research. Elsevier, 2019. <a href=\"https://doi.org/10.1016/bs.aivir.2019.07.008\">https://doi.org/10.1016/bs.aivir.2019.07.008</a>.","ieee":"M. Obr and F. K. Schur, “Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging,” in <i>Complementary Strategies to Study Virus Structure and Function</i>, vol. 105, F. A. Rey, Ed. Elsevier, 2019, pp. 117–159.","ista":"Obr M, Schur FK. 2019.Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging. In: Complementary Strategies to Study Virus Structure and Function. vol. 105, 117–159.","apa":"Obr, M., &#38; Schur, F. K. (2019). Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging. In F. A. Rey (Ed.), <i>Complementary Strategies to Study Virus Structure and Function</i> (Vol. 105, pp. 117–159). Elsevier. <a href=\"https://doi.org/10.1016/bs.aivir.2019.07.008\">https://doi.org/10.1016/bs.aivir.2019.07.008</a>","ama":"Obr M, Schur FK. Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging. In: Rey FA, ed. <i>Complementary Strategies to Study Virus Structure and Function</i>. Vol 105. Advances in Virus Research. Elsevier; 2019:117-159. doi:<a href=\"https://doi.org/10.1016/bs.aivir.2019.07.008\">10.1016/bs.aivir.2019.07.008</a>","mla":"Obr, Martin, and Florian KM Schur. “Structural Analysis of Pleomorphic and Asymmetric Viruses Using Cryo-Electron Tomography and Subtomogram Averaging.” <i>Complementary Strategies to Study Virus Structure and Function</i>, edited by Félix A. Rey, vol. 105, Elsevier, 2019, pp. 117–59, doi:<a href=\"https://doi.org/10.1016/bs.aivir.2019.07.008\">10.1016/bs.aivir.2019.07.008</a>.","short":"M. Obr, F.K. Schur, in:, F.A. Rey (Ed.), Complementary Strategies to Study Virus Structure and Function, Elsevier, 2019, pp. 117–159."},"department":[{"_id":"FlSc"}],"publication_status":"published","series_title":"Advances in Virus Research","article_processing_charge":"No","oa_version":"None","abstract":[{"lang":"eng","text":"Describing the protein interactions that form pleomorphic and asymmetric viruses represents a considerable challenge to most structural biology techniques, including X-ray crystallography and single particle cryo-electron microscopy. Obtaining a detailed understanding of these interactions is nevertheless important, considering the number of relevant human pathogens that do not follow strict icosahedral or helical symmetry. Cryo-electron tomography and subtomogram averaging methods provide structural insights into complex biological environments and are well suited to go beyond structures of perfectly symmetric viruses. This chapter discusses recent developments showing that cryo-ET and subtomogram averaging can provide high-resolution insights into hitherto unknown structural features of pleomorphic and asymmetric virus particles. It also describes how these methods have significantly added to our understanding of retrovirus capsid assemblies in immature and mature viruses. Additional examples of irregular viruses and their associated proteins, whose structures have been studied via cryo-ET and subtomogram averaging, further support the versatility of these methods."}],"scopus_import":"1","year":"2019","date_updated":"2023-08-30T06:56:00Z","isi":1,"month":"08","date_published":"2019-08-27T00:00:00Z","publisher":"Elsevier"},{"oa_version":"Submitted Version","article_processing_charge":"No","publication_status":"published","publisher":"Nature Publishing Group","date_published":"2018-08-29T00:00:00Z","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242333/","open_access":"1"}],"month":"08","isi":1,"date_updated":"2023-09-12T07:44:37Z","scopus_import":"1","abstract":[{"lang":"eng","text":"A short, 14-amino-acid segment called SP1, located in the Gag structural protein1, has a critical role during the formation of the HIV-1 virus particle. During virus assembly, the SP1 peptide and seven preceding residues fold into a six-helix bundle, which holds together the Gag hexamer and facilitates the formation of a curved immature hexagonal lattice underneath the viral membrane2,3. Upon completion of assembly and budding, proteolytic cleavage of Gag leads to virus maturation, in which the immature lattice is broken down; the liberated CA domain of Gag then re-assembles into the mature conical capsid that encloses the viral genome and associated enzymes. Folding and proteolysis of the six-helix bundle are crucial rate-limiting steps of both Gag assembly and disassembly, and the six-helix bundle is an established target of HIV-1 inhibitors4,5. Here, using a combination of structural and functional analyses, we show that inositol hexakisphosphate (InsP6, also known as IP6) facilitates the formation of the six-helix bundle and assembly of the immature HIV-1 Gag lattice. IP6 makes ionic contacts with two rings of lysine residues at the centre of the Gag hexamer. Proteolytic cleavage then unmasks an alternative binding site, where IP6 interaction promotes the assembly of the mature capsid lattice. These studies identify IP6 as a naturally occurring small molecule that promotes both assembly and maturation of HIV-1."}],"year":"2018","day":"29","_id":"150","publication":"Nature","issue":"7719","type":"journal_article","citation":{"short":"R. Dick, K.K. Zadrozny, C. Xu, F.K. Schur, T.D. Lyddon, C.L. Ricana, J.M. Wagner, J.R. Perilla, P.B.K. Ganser, M.C. Johnson, O. Pornillos, V. Vogt, Nature 560 (2018) 509–512.","ama":"Dick R, Zadrozny KK, Xu C, et al. Inositol phosphates are assembly co-factors for HIV-1. <i>Nature</i>. 2018;560(7719):509–512. doi:<a href=\"https://doi.org/10.1038/s41586-018-0396-4\">10.1038/s41586-018-0396-4</a>","mla":"Dick, Robert, et al. “Inositol Phosphates Are Assembly Co-Factors for HIV-1.” <i>Nature</i>, vol. 560, no. 7719, Nature Publishing Group, 2018, pp. 509–512, doi:<a href=\"https://doi.org/10.1038/s41586-018-0396-4\">10.1038/s41586-018-0396-4</a>.","ista":"Dick R, Zadrozny KK, Xu C, Schur FK, Lyddon TD, Ricana CL, Wagner JM, Perilla JR, Ganser PBK, Johnson MC, Pornillos O, Vogt V. 2018. Inositol phosphates are assembly co-factors for HIV-1. Nature. 560(7719), 509–512.","apa":"Dick, R., Zadrozny, K. K., Xu, C., Schur, F. K., Lyddon, T. D., Ricana, C. L., … Vogt, V. (2018). Inositol phosphates are assembly co-factors for HIV-1. <i>Nature</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/s41586-018-0396-4\">https://doi.org/10.1038/s41586-018-0396-4</a>","ieee":"R. Dick <i>et al.</i>, “Inositol phosphates are assembly co-factors for HIV-1,” <i>Nature</i>, vol. 560, no. 7719. Nature Publishing Group, pp. 509–512, 2018.","chicago":"Dick, Robert, Kaneil K Zadrozny, Chaoyi Xu, Florian KM Schur, Terri D Lyddon, Clifton L Ricana, Jonathan M Wagner, et al. “Inositol Phosphates Are Assembly Co-Factors for HIV-1.” <i>Nature</i>. Nature Publishing Group, 2018. <a href=\"https://doi.org/10.1038/s41586-018-0396-4\">https://doi.org/10.1038/s41586-018-0396-4</a>."},"department":[{"_id":"FlSc"}],"oa":1,"publication_identifier":{"eissn":["1476-4687"]},"doi":"10.1038/s41586-018-0396-4","pmid":1,"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","date_created":"2018-12-11T11:44:53Z","article_type":"original","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41586-018-0505-4"}]},"volume":560,"page":"509–512","title":"Inositol phosphates are assembly co-factors for HIV-1","quality_controlled":"1","external_id":{"pmid":["30158708"],"isi":["000442483400046"]},"author":[{"full_name":"Dick, Robert","first_name":"Robert","last_name":"Dick"},{"first_name":"Kaneil K","full_name":"Zadrozny, Kaneil K","last_name":"Zadrozny"},{"first_name":"Chaoyi","full_name":"Xu, Chaoyi","last_name":"Xu"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","last_name":"Schur","full_name":"Schur, Florian","first_name":"Florian"},{"last_name":"Lyddon","first_name":"Terri D","full_name":"Lyddon, Terri D"},{"last_name":"Ricana","first_name":"Clifton L","full_name":"Ricana, Clifton L"},{"full_name":"Wagner, Jonathan M","first_name":"Jonathan M","last_name":"Wagner"},{"first_name":"Juan R","full_name":"Perilla, Juan R","last_name":"Perilla"},{"full_name":"Ganser, Pornillos Barbie K","first_name":"Pornillos Barbie K","last_name":"Ganser"},{"first_name":"Marc C","full_name":"Johnson, Marc C","last_name":"Johnson"},{"last_name":"Pornillos","first_name":"Owen","full_name":"Pornillos, Owen"},{"full_name":"Vogt, Volker","first_name":"Volker","last_name":"Vogt"}],"language":[{"iso":"eng"}],"status":"public","intvolume":"       560"},{"date_updated":"2025-06-03T11:56:09Z","month":"12","isi":1,"abstract":[{"text":"Retroviruses assemble and bud from infected cells in an immature form and require proteolytic maturation for infectivity. The CA (capsid) domains of the Gag polyproteins assemble a protein lattice as a truncated sphere in the immature virion. Proteolytic cleavage of Gag induces dramatic structural rearrangements; a subset of cleaved CA subsequently assembles into the mature core, whose architecture varies among retroviruses. Murine leukemia virus (MLV) is the prototypical γ-retrovirus and serves as the basis of retroviral vectors, but the structure of the MLV CA layer is unknown. Here we have combined X-ray crystallography with cryoelectron tomography to determine the structures of immature and mature MLV CA layers within authentic viral particles. This reveals the structural changes associated with maturation, and, by comparison with HIV-1, uncovers conserved and variable features. In contrast to HIV-1, most MLV CA is used for assembly of the mature core, which adopts variable, multilayered morphologies and does not form a closed structure. Unlike in HIV-1, there is similarity between protein–protein interfaces in the immature MLV CA layer and those in the mature CA layer, and structural maturation of MLV could be achieved through domain rotations that largely maintain hexameric interactions. Nevertheless, the dramatic architectural change on maturation indicates that extensive disassembly and reassembly are required for mature core growth. The core morphology suggests that wrapping of the genome in CA sheets may be sufficient to protect the MLV ribonucleoprotein during cell entry.","lang":"eng"}],"scopus_import":"1","year":"2018","date_published":"2018-12-11T00:00:00Z","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pubmed/30478053","open_access":"1"}],"publisher":"National Academy of Sciences","article_processing_charge":"No","publication_status":"published","oa_version":"Submitted Version","doi":"10.1073/pnas.1811580115","publication_identifier":{"issn":["0027-8424"]},"type":"journal_article","department":[{"_id":"FlSc"}],"citation":{"ieee":"K. Qu <i>et al.</i>, “Structure and architecture of immature and mature murine leukemia virus capsids,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 115, no. 50. National Academy of Sciences, pp. E11751–E11760, 2018.","chicago":"Qu, Kun, Bärbel Glass, Michal Doležal, Florian KM Schur, Brice Murciano, Alan Rein, Michaela Rumlová, Tomáš Ruml, Hans-Georg Kräusslich, and John A. G. Briggs. “Structure and Architecture of Immature and Mature Murine Leukemia Virus Capsids.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2018. <a href=\"https://doi.org/10.1073/pnas.1811580115\">https://doi.org/10.1073/pnas.1811580115</a>.","mla":"Qu, Kun, et al. “Structure and Architecture of Immature and Mature Murine Leukemia Virus Capsids.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 115, no. 50, National Academy of Sciences, 2018, pp. E11751–60, doi:<a href=\"https://doi.org/10.1073/pnas.1811580115\">10.1073/pnas.1811580115</a>.","ama":"Qu K, Glass B, Doležal M, et al. Structure and architecture of immature and mature murine leukemia virus capsids. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2018;115(50):E11751-E11760. doi:<a href=\"https://doi.org/10.1073/pnas.1811580115\">10.1073/pnas.1811580115</a>","short":"K. Qu, B. Glass, M. Doležal, F.K. Schur, B. Murciano, A. Rein, M. Rumlová, T. Ruml, H.-G. Kräusslich, J.A.G. Briggs, Proceedings of the National Academy of Sciences of the United States of America 115 (2018) E11751–E11760.","ista":"Qu K, Glass B, Doležal M, Schur FK, Murciano B, Rein A, Rumlová M, Ruml T, Kräusslich H-G, Briggs JAG. 2018. Structure and architecture of immature and mature murine leukemia virus capsids. Proceedings of the National Academy of Sciences of the United States of America. 115(50), E11751–E11760.","apa":"Qu, K., Glass, B., Doležal, M., Schur, F. K., Murciano, B., Rein, A., … Briggs, J. A. G. (2018). Structure and architecture of immature and mature murine leukemia virus capsids. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1811580115\">https://doi.org/10.1073/pnas.1811580115</a>"},"oa":1,"publication":"Proceedings of the National Academy of Sciences of the United States of America","issue":"50","day":"11","_id":"5770","volume":115,"date_created":"2018-12-20T21:09:37Z","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","intvolume":"       115","language":[{"iso":"eng"}],"author":[{"last_name":"Qu","first_name":"Kun","full_name":"Qu, Kun"},{"last_name":"Glass","first_name":"Bärbel","full_name":"Glass, Bärbel"},{"last_name":"Doležal","first_name":"Michal","full_name":"Doležal, Michal"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","last_name":"Schur","full_name":"Schur, Florian","first_name":"Florian"},{"first_name":"Brice","full_name":"Murciano, Brice","last_name":"Murciano"},{"full_name":"Rein, Alan","first_name":"Alan","last_name":"Rein"},{"last_name":"Rumlová","full_name":"Rumlová, Michaela","first_name":"Michaela"},{"last_name":"Ruml","first_name":"Tomáš","full_name":"Ruml, Tomáš"},{"last_name":"Kräusslich","full_name":"Kräusslich, Hans-Georg","first_name":"Hans-Georg"},{"last_name":"Briggs","first_name":"John A. G.","full_name":"Briggs, John A. G."}],"external_id":{"isi":["000452866000022"],"pmid":["30478053"]},"quality_controlled":"1","title":"Structure and architecture of immature and mature murine leukemia virus capsids","page":"E11751-E11760"}]