[{"date_published":"2024-12-30T00:00:00Z","file_date_updated":"2025-01-07T12:15:14Z","citation":{"ista":"Datler J. 2024. Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM. Institute of Science and Technology Austria.","short":"J. Datler, Elucidating the Structural Determinants of the Poxvirus Core Using Multi-Modal Cryo-EM, Institute of Science and Technology Austria, 2024.","chicago":"Datler, Julia. “Elucidating the Structural Determinants of the Poxvirus Core Using Multi-Modal Cryo-EM.” Institute of Science and Technology Austria, 2024. <a href=\"https://doi.org/10.15479/at:ista:18766\">https://doi.org/10.15479/at:ista:18766</a>.","ama":"Datler J. Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM. 2024. doi:<a href=\"https://doi.org/10.15479/at:ista:18766\">10.15479/at:ista:18766</a>","apa":"Datler, J. (2024). <i>Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/at:ista:18766\">https://doi.org/10.15479/at:ista:18766</a>","ieee":"J. Datler, “Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM,” Institute of Science and Technology Austria, 2024.","mla":"Datler, Julia. <i>Elucidating the Structural Determinants of the Poxvirus Core Using Multi-Modal Cryo-EM</i>. Institute of Science and Technology Austria, 2024, doi:<a href=\"https://doi.org/10.15479/at:ista:18766\">10.15479/at:ista:18766</a>."},"oa":1,"month":"12","article_processing_charge":"No","date_created":"2025-01-07T10:23:12Z","publication_identifier":{"issn":["2663-337X"],"isbn":["978-3-99078-049-7"]},"language":[{"iso":"eng"}],"year":"2024","_id":"18766","page":"106","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"ScienComp"}],"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","date_updated":"2026-04-07T12:59:44Z","status":"public","type":"dissertation","publisher":"Institute of Science and Technology Austria","keyword":["cryo-EM","cryo-ET","cryo-SPA","Structural Virology","Poxvirus","Vaccinia Virus","Structural Biology"],"supervisor":[{"orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur"}],"acknowledgement":"This work was funded by the Austrian Science Fund (FWF) grant P31445 and ISTA. I\r\nwould like to express my gratitude to the Scientific Service Units, particularly the Lab\r\nSupport Facility, the Scientific Computing Facility and the Electron Microscopy Facility\r\nfor their tremendous support. I want to especially thank Alois for assisting me with the\r\ninstallation of countless new software and for troubleshooting cluster issues. A special\r\nthanks goes to Valentin for his outstanding support in cryo-EM data acquisition and\r\nhis ongoing help in improving the process to ensure that I obtained the best possible\r\ndata from my sample.","doi":"10.15479/at:ista:18766","title":"Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png"},"department":[{"_id":"GradSch"},{"_id":"FlSc"}],"file":[{"content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","file_size":38814932,"file_id":"18769","creator":"jstanger","checksum":"3e51cab327c754045c3d29c1a50cc9a9","access_level":"closed","date_updated":"2025-01-07T12:15:11Z","relation":"source_file","date_created":"2025-01-07T12:15:11Z","file_name":"PhD_thesis_Julia_Datler.docx"},{"file_size":12044865,"content_type":"application/pdf","relation":"main_file","date_updated":"2025-01-07T12:15:14Z","access_level":"open_access","date_created":"2025-01-07T12:15:14Z","creator":"jstanger","checksum":"22fabe5b97950bf852212f6edb555173","file_id":"18770","success":1,"file_name":"PhD_thesis_Julia_Datler.pdf"}],"degree_awarded":"PhD","author":[{"orcid":"0000-0002-3616-8580","id":"3B12E2E6-F248-11E8-B48F-1D18A9856A87","full_name":"Datler, Julia","first_name":"Julia","last_name":"Datler"}],"oa_version":"Published Version","abstract":[{"text":"Poxviruses are large pleomorphic double-stranded DNA viruses that include well known members such as variola virus, the causative agent of smallpox, Mpox virus, as well as Vaccinia virus (VACV), which serves as a vaccination strain for formerly mentioned viruses. VACV is a valuable model for studying large pleomorphic DNA viruses in general and poxviruses specifically, as many features, such as core morphology and structural proteins, are well conserved within this family. Despite decades of research, our understanding of the structural components and proteins that comprise the poxvirus core in mature virions remains limited. Although major core proteins were identified via indirect experimental evidence, the core's complexity, with its large size, structure and number of involved proteins, has hindered efforts to achieve high-resolution insights and to define the roles of the individual proteins. The specific protein composition of the core's individual layers, including the palisade layer and the inner core wall, has remained unclear. In this study, we have merged multiple approaches, including single particle cryo electron microscopy of purified virus cores, cryo-electron tomography and subtomogram averaging of mature virions and molecular modeling to elucidate the structural determinants of the VACV core. Due to the lack of experimentally derived structures, either in situ or reconstituted in vitro, we used Alphafold to predict models of the putative major core protein candidates, A10, 23k, A3, A4, and L4. Our results show that the VACV core is composed of several layers with varying local symmetries, forming more intricate interactions than observed previously. This allowed us to identify several molecular building blocks forming the viral core lattice. In particular, we identified trimers of protein A10 as a major core structure that forms the palisade layer of the viral core. Additionally, we revealed that six petals of a flower shaped core pore within the core wall are composed of A10 trimers. Furthermore, we obtained a cryo-EM density for the inner core wall that could potentially accommodate an A3 dimer. Integrating descriptions of protein interactions from previous studies enabled us to provide a detailed structural model of the poxvirus core wall, and our findings indicate that the interactions within A10 trimers are likely consistent across orthopox- and parapoxviruses. This combined application of cryo-SPA and cryo-ET can help overcome obstacles in studying complex virus structures in the future, including their key assembly proteins, interactions, and the formation into a core lattice. Our work provides important fundamental new insights into poxvirus core architecture, also considering the recent re-emergence of poxviruses.","lang":"eng"}],"day":"30","ddc":["570"],"project":[{"_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid","call_identifier":"FWF","grant_number":"P31445"}],"publication_status":"published","corr_author":"1","OA_place":"publisher","has_accepted_license":"1","related_material":{"record":[{"id":"12334","status":"public","relation":"part_of_dissertation"},{"status":"public","relation":"part_of_dissertation","id":"14979"}]},"alternative_title":["ISTA thesis"]},{"date_published":"2022-03-01T00:00:00Z","citation":{"apa":"Windhaber, S., Xin, Q., Uckeley, Z. M., Koch, J., Obr, M., Garnier, C., … Lozach, P.-Y. (2022). The Orthobunyavirus Germiston enters host cells from late endosomes. <i>Journal of Virology</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/jvi.02146-21\">https://doi.org/10.1128/jvi.02146-21</a>","ieee":"S. Windhaber <i>et al.</i>, “The Orthobunyavirus Germiston enters host cells from late endosomes,” <i>Journal of Virology</i>, vol. 96, no. 5. American Society for Microbiology, 2022.","mla":"Windhaber, Stefan, et al. “The Orthobunyavirus Germiston Enters Host Cells from Late Endosomes.” <i>Journal of Virology</i>, vol. 96, no. 5, e02146-21, American Society for Microbiology, 2022, doi:<a href=\"https://doi.org/10.1128/jvi.02146-21\">10.1128/jvi.02146-21</a>.","chicago":"Windhaber, Stefan, Qilin Xin, Zina M. Uckeley, Jana Koch, Martin Obr, Céline Garnier, Catherine Luengo-Guyonnot, Maëva Duboeuf, Florian KM Schur, and Pierre-Yves Lozach. “The Orthobunyavirus Germiston Enters Host Cells from Late Endosomes.” <i>Journal of Virology</i>. American Society for Microbiology, 2022. <a href=\"https://doi.org/10.1128/jvi.02146-21\">https://doi.org/10.1128/jvi.02146-21</a>.","ama":"Windhaber S, Xin Q, Uckeley ZM, et al. The Orthobunyavirus Germiston enters host cells from late endosomes. <i>Journal of Virology</i>. 2022;96(5). doi:<a href=\"https://doi.org/10.1128/jvi.02146-21\">10.1128/jvi.02146-21</a>","ista":"Windhaber S, Xin Q, Uckeley ZM, Koch J, Obr M, Garnier C, Luengo-Guyonnot C, Duboeuf M, Schur FK, Lozach P-Y. 2022. The Orthobunyavirus Germiston enters host cells from late endosomes. Journal of Virology. 96(5), e02146-21.","short":"S. Windhaber, Q. Xin, Z.M. Uckeley, J. Koch, M. Obr, C. Garnier, C. Luengo-Guyonnot, M. Duboeuf, F.K. Schur, P.-Y. Lozach, Journal of Virology 96 (2022)."},"month":"03","volume":96,"article_processing_charge":"No","oa":1,"date_created":"2022-01-18T10:04:18Z","quality_controlled":"1","publication_identifier":{"eissn":["1098-5514"],"issn":["0022-538X"]},"language":[{"iso":"eng"}],"pmid":1,"year":"2022","acknowledged_ssus":[{"_id":"EM-Fac"}],"_id":"10639","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_type":"original","isi":1,"intvolume":"        96","publisher":"American Society for Microbiology","type":"journal_article","keyword":["virology","insect science","immunology","microbiology"],"status":"public","date_updated":"2025-04-15T08:24:49Z","doi":"10.1128/jvi.02146-21","acknowledgement":"This work  was  supported  by  INRAE  starter  funds, Project IDEXLYON  (University  of  Lyon) within  the  Programme  Investissements  d’Avenir  (ANR-16-IDEX-0005),  and  FINOVIAO14 (Fondation  pour  l’Université  de  Lyon),  all  to  P.Y.L.  This  work  was  also  supported  by CellNetworks  Research  Group  funds  and  Deutsche  Forschungsgemeinschaft  (DFG)  funding (grant  numbers  LO-2338/1-1  and  LO-2338/3-1)  awarded  to  P.Y.L., Austrian  Science  Fund (FWF)  grant  P31445  to  F.K.M.S., a  Chinese  Scholarship  Council (CSC;no.  201904910701) fellowship  to   Q.X.,  and  a  ministére  de  l’enseignement  supérieur,  de  la  recherche  et  de l’innovation (MESRI) doctoral thesis grant to M.D.","title":"The Orthobunyavirus Germiston enters host cells from late endosomes","department":[{"_id":"FlSc"}],"main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8906410"}],"external_id":{"pmid":["35019710"],"isi":["000779305000033"]},"author":[{"first_name":"Stefan","last_name":"Windhaber","full_name":"Windhaber, Stefan"},{"first_name":"Qilin","full_name":"Xin, Qilin","last_name":"Xin"},{"full_name":"Uckeley, Zina M.","last_name":"Uckeley","first_name":"Zina M."},{"full_name":"Koch, Jana","last_name":"Koch","first_name":"Jana"},{"orcid":"0000-0003-1756-6564","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","full_name":"Obr, Martin","last_name":"Obr","first_name":"Martin"},{"first_name":"Céline","full_name":"Garnier, Céline","last_name":"Garnier"},{"last_name":"Luengo-Guyonnot","full_name":"Luengo-Guyonnot, Catherine","first_name":"Catherine"},{"last_name":"Duboeuf","first_name":"Maëva","full_name":"Duboeuf, Maëva"},{"orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Lozach, Pierre-Yves","last_name":"Lozach","first_name":"Pierre-Yves"}],"oa_version":"Published Version","project":[{"grant_number":"P31445","name":"Structural conservation and diversity in retroviral capsid","call_identifier":"FWF","_id":"26736D6A-B435-11E9-9278-68D0E5697425"}],"abstract":[{"lang":"eng","text":"With more than 80 members worldwide, the Orthobunyavirus genus in the Peribunyaviridae family is a large genus of enveloped RNA viruses, many of which are emerging pathogens in humans and livestock. How orthobunyaviruses (OBVs) penetrate and infect mammalian host cells remains poorly characterized. Here, we investigated the entry mechanisms of the OBV Germiston (GERV). Viral particles were visualized by cryo-electron microscopy and appeared roughly spherical with an average diameter of 98 nm. Labeling of the virus with fluorescent dyes did not adversely affect its infectivity and allowed the monitoring of single particles in fixed and live cells. Using this approach, we found that endocytic internalization of bound viruses was asynchronous and occurred within 30-40 min. The virus entered Rab5a+ early endosomes and, subsequently, late endosomal vacuoles containing Rab7a but not LAMP-1. Infectious entry did not require proteolytic cleavage, and endosomal acidification was sufficient and necessary for viral fusion. Acid-activated penetration began 15-25 min after initiation of virus internalization and relied on maturation of early endosomes to late endosomes. The optimal pH for viral membrane fusion was slightly below 6.0, and penetration was hampered when the potassium influx was abolished. Overall, our study provides real-time visualization of GERV entry into host cells and demonstrates the importance of late endosomal maturation in facilitating OBV penetration."}],"day":"01","issue":"5","publication":"Journal of Virology","scopus_import":"1","publication_status":"published","article_number":"e02146-21"},{"citation":{"ista":"Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. 2021. Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. mBio. 12(4), 676.","short":"D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, M. Kim, MBio 12 (2021).","apa":"Le, D., Krasnopeeva, E., Sinjab, F., Pilizota, T., &#38; Kim, M. (2021). Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. <i>MBio</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/mbio.00676-21\">https://doi.org/10.1128/mbio.00676-21</a>","ieee":"D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, and M. Kim, “Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria,” <i>mBio</i>, vol. 12, no. 4. American Society for Microbiology, 2021.","mla":"Le, Dai, et al. “Active Efflux Leads to Heterogeneous Dissipation of Proton Motive Force by Protonophores in Bacteria.” <i>MBio</i>, vol. 12, no. 4, 676, American Society for Microbiology, 2021, doi:<a href=\"https://doi.org/10.1128/mbio.00676-21\">10.1128/mbio.00676-21</a>.","ama":"Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. <i>mBio</i>. 2021;12(4). doi:<a href=\"https://doi.org/10.1128/mbio.00676-21\">10.1128/mbio.00676-21</a>","chicago":"Le, Dai, Ekaterina Krasnopeeva, Faris Sinjab, Teuta Pilizota, and Minsu Kim. “Active Efflux Leads to Heterogeneous Dissipation of Proton Motive Force by Protonophores in Bacteria.” <i>MBio</i>. American Society for Microbiology, 2021. <a href=\"https://doi.org/10.1128/mbio.00676-21\">https://doi.org/10.1128/mbio.00676-21</a>."},"oa":1,"month":"08","article_processing_charge":"Yes","volume":12,"date_published":"2021-08-31T00:00:00Z","file_date_updated":"2024-04-10T09:05:49Z","quality_controlled":"1","publication_identifier":{"issn":["2150-7511"]},"language":[{"iso":"eng"}],"date_created":"2024-04-03T07:51:57Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","pmid":1,"year":"2021","_id":"15270","doi":"10.1128/mbio.00676-21","intvolume":"        12","date_updated":"2024-04-10T09:13:59Z","publisher":"American Society for Microbiology","keyword":["Virology","Microbiology"],"status":"public","type":"journal_article","department":[{"_id":"CaGu"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"file":[{"content_type":"application/pdf","file_size":1344204,"success":1,"file_name":"2021_mBio_Le.pdf","file_id":"15309","creator":"dernst","checksum":"529e3f97ae5c5f5cc743c4fc130c9440","access_level":"open_access","relation":"main_file","date_updated":"2024-04-10T09:05:49Z","date_created":"2024-04-10T09:05:49Z"}],"title":"Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria","author":[{"last_name":"Le","full_name":"Le, Dai","first_name":"Dai"},{"first_name":"Ekaterina","full_name":"Krasnopeeva, Ekaterina","id":"1F1EE44A-BF83-11EA-B3C1-BB9CC619BF3A","last_name":"Krasnopeeva"},{"first_name":"Faris","last_name":"Sinjab","full_name":"Sinjab, Faris"},{"last_name":"Pilizota","first_name":"Teuta","full_name":"Pilizota, Teuta"},{"last_name":"Kim","full_name":"Kim, Minsu","first_name":"Minsu"}],"external_id":{"pmid":["34253054"]},"day":"31","abstract":[{"text":"Various toxic compounds disrupt bacterial physiology. While bacteria harbor defense mechanisms to mitigate the toxicity, these mechanisms are often coupled to the physiological state of the cells and become ineffective when the physiology is severely disrupted.","lang":"eng"}],"ddc":["570"],"issue":"4","publication":"mBio","oa_version":"Published Version","has_accepted_license":"1","article_number":"676","publication_status":"published"},{"pmid":1,"year":"2021","_id":"15274","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","intvolume":"        12","type":"journal_article","keyword":["Virology","Microbiology"],"status":"public","publisher":"American Society for Microbiology","date_updated":"2024-04-09T10:47:16Z","doi":"10.1128/mbio.01567-21","date_published":"2021-08-31T00:00:00Z","file_date_updated":"2024-04-09T10:45:11Z","citation":{"ista":"Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. 2021. Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. mBio. 12(4), e01567.","short":"B. Khalfaoui-Hassani, P.I. Trasnea, S. Steimle, H.-G. Koch, F. Daldal, MBio 12 (2021).","ama":"Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. <i>mBio</i>. 2021;12(4). doi:<a href=\"https://doi.org/10.1128/mbio.01567-21\">10.1128/mbio.01567-21</a>","chicago":"Khalfaoui-Hassani, Bahia, Petru Iulian Trasnea, Stefan Steimle, Hans-Georg Koch, and Fevzi Daldal. “Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide Insight into Copper Import.” <i>MBio</i>. American Society for Microbiology, 2021. <a href=\"https://doi.org/10.1128/mbio.01567-21\">https://doi.org/10.1128/mbio.01567-21</a>.","apa":"Khalfaoui-Hassani, B., Trasnea, P. I., Steimle, S., Koch, H.-G., &#38; Daldal, F. (2021). Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. <i>MBio</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/mbio.01567-21\">https://doi.org/10.1128/mbio.01567-21</a>","mla":"Khalfaoui-Hassani, Bahia, et al. “Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide Insight into Copper Import.” <i>MBio</i>, vol. 12, no. 4, e01567, American Society for Microbiology, 2021, doi:<a href=\"https://doi.org/10.1128/mbio.01567-21\">10.1128/mbio.01567-21</a>.","ieee":"B. Khalfaoui-Hassani, P. I. Trasnea, S. Steimle, H.-G. Koch, and F. Daldal, “Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import,” <i>mBio</i>, vol. 12, no. 4. American Society for Microbiology, 2021."},"article_processing_charge":"No","month":"08","volume":12,"oa":1,"date_created":"2024-04-03T07:59:04Z","publication_identifier":{"issn":["2150-7511"]},"quality_controlled":"1","language":[{"iso":"eng"}],"oa_version":"Published Version","ddc":["570"],"abstract":[{"lang":"eng","text":"Copper (Cu) is a redox-active micronutrient that is both essential and toxic. Its cellular homeostasis is critical for supporting cuproprotein maturation while avoiding excessive oxidative stress. The Cu importer CcoA is the prototype of the widespread CalT subfamily of the MFS-type transporters. Hence, understanding its molecular mechanism of function is significant. Here, we show that CcoA undergoes a thiol:disulfide oxidoreduction cycle, which is important for its Cu import activity."}],"day":"31","issue":"4","publication":"mBio","publication_status":"published","has_accepted_license":"1","article_number":"e01567","title":"Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"department":[{"_id":"LeSa"}],"file":[{"file_name":"2021_mBio_KhalfaouiHassani.pdf","success":1,"creator":"dernst","checksum":"2f6a57637cb3162eaeeb155a5b031e76","file_id":"15306","access_level":"open_access","date_updated":"2024-04-09T10:45:11Z","relation":"main_file","date_created":"2024-04-09T10:45:11Z","content_type":"application/pdf","file_size":3383398}],"external_id":{"pmid":["34281385"]},"author":[{"last_name":"Khalfaoui-Hassani","first_name":"Bahia","full_name":"Khalfaoui-Hassani, Bahia"},{"last_name":"Trasnea","first_name":"Petru Iulian","id":"D560034C-10C4-11EA-ABF4-A4B43DDC885E","full_name":"Trasnea, Petru Iulian"},{"full_name":"Steimle, Stefan","first_name":"Stefan","last_name":"Steimle"},{"first_name":"Hans-Georg","full_name":"Koch, Hans-Georg","last_name":"Koch"},{"first_name":"Fevzi","last_name":"Daldal","full_name":"Daldal, Fevzi"}]},{"date_created":"2024-04-03T08:00:34Z","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1553-7374"]},"quality_controlled":"1","file_date_updated":"2024-04-09T10:24:43Z","date_published":"2021-06-24T00:00:00Z","article_processing_charge":"Yes","volume":17,"month":"06","oa":1,"citation":{"ama":"Navarrete F, Grujic N, Stirnberg A, et al. The Pleiades are a cluster of fungal effectors that inhibit host defenses. <i>PLOS Pathogens</i>. 2021;17(6). doi:<a href=\"https://doi.org/10.1371/journal.ppat.1009641\">10.1371/journal.ppat.1009641</a>","chicago":"Navarrete, Fernando, Nenad Grujic, Alexandra Stirnberg, Indira Saado, David Aleksza, Michelle C Gallei, Hazem Adi, et al. “The Pleiades Are a Cluster of Fungal Effectors That Inhibit Host Defenses.” <i>PLOS Pathogens</i>. Public Library of Science, 2021. <a href=\"https://doi.org/10.1371/journal.ppat.1009641\">https://doi.org/10.1371/journal.ppat.1009641</a>.","ieee":"F. Navarrete <i>et al.</i>, “The Pleiades are a cluster of fungal effectors that inhibit host defenses,” <i>PLOS Pathogens</i>, vol. 17, no. 6. Public Library of Science, 2021.","mla":"Navarrete, Fernando, et al. “The Pleiades Are a Cluster of Fungal Effectors That Inhibit Host Defenses.” <i>PLOS Pathogens</i>, vol. 17, no. 6, e1009641, Public Library of Science, 2021, doi:<a href=\"https://doi.org/10.1371/journal.ppat.1009641\">10.1371/journal.ppat.1009641</a>.","apa":"Navarrete, F., Grujic, N., Stirnberg, A., Saado, I., Aleksza, D., Gallei, M. C., … Djamei, A. (2021). The Pleiades are a cluster of fungal effectors that inhibit host defenses. <i>PLOS Pathogens</i>. Public Library of Science. <a href=\"https://doi.org/10.1371/journal.ppat.1009641\">https://doi.org/10.1371/journal.ppat.1009641</a>","short":"F. Navarrete, N. Grujic, A. Stirnberg, I. Saado, D. Aleksza, M.C. Gallei, H. Adi, A. Alcântara, M. Khan, J. Bindics, M. Trujillo, A. Djamei, PLOS Pathogens 17 (2021).","ista":"Navarrete F, Grujic N, Stirnberg A, Saado I, Aleksza D, Gallei MC, Adi H, Alcântara A, Khan M, Bindics J, Trujillo M, Djamei A. 2021. The Pleiades are a cluster of fungal effectors that inhibit host defenses. PLOS Pathogens. 17(6), e1009641."},"status":"public","type":"journal_article","keyword":["Virology","Genetics","Molecular Biology","Immunology","Microbiology","Parasitology"],"publisher":"Public Library of Science","date_updated":"2024-04-09T10:26:12Z","intvolume":"        17","doi":"10.1371/journal.ppat.1009641","_id":"15276","year":"2021","pmid":1,"article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"pmid":["34166468"]},"author":[{"last_name":"Navarrete","first_name":"Fernando","full_name":"Navarrete, Fernando"},{"full_name":"Grujic, Nenad","first_name":"Nenad","last_name":"Grujic"},{"full_name":"Stirnberg, Alexandra","last_name":"Stirnberg","first_name":"Alexandra"},{"full_name":"Saado, Indira","first_name":"Indira","last_name":"Saado"},{"full_name":"Aleksza, David","first_name":"David","last_name":"Aleksza"},{"orcid":"0000-0003-1286-7368","full_name":"Gallei, Michelle C","first_name":"Michelle C","id":"35A03822-F248-11E8-B48F-1D18A9856A87","last_name":"Gallei"},{"last_name":"Adi","first_name":"Hazem","full_name":"Adi, Hazem"},{"first_name":"André","last_name":"Alcântara","full_name":"Alcântara, André"},{"last_name":"Khan","first_name":"Mamoona","full_name":"Khan, Mamoona"},{"full_name":"Bindics, Janos","first_name":"Janos","last_name":"Bindics"},{"first_name":"Marco","full_name":"Trujillo, Marco","last_name":"Trujillo"},{"full_name":"Djamei, Armin","first_name":"Armin","last_name":"Djamei"}],"title":"The Pleiades are a cluster of fungal effectors that inhibit host defenses","file":[{"file_size":2616563,"content_type":"application/pdf","success":1,"file_name":"2021_PlosPathogens_Navarrete.pdf","relation":"main_file","access_level":"open_access","date_updated":"2024-04-09T10:24:43Z","date_created":"2024-04-09T10:24:43Z","creator":"dernst","file_id":"15305","checksum":"ab8428291a0c14607c4ea5656c029cff"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"department":[{"_id":"JiFr"}],"publication_status":"published","article_number":"e1009641","has_accepted_license":"1","oa_version":"Published Version","publication":"PLOS Pathogens","issue":"6","abstract":[{"text":"Biotrophic plant pathogens secrete effector proteins to manipulate the host physiology. Effectors suppress defenses and induce an environment favorable to disease development. Sequence-based prediction of effector function is impeded by their rapid evolution rate. In the maize pathogen <jats:italic>Ustilago maydis</jats:italic>, effector-coding genes frequently organize in clusters. Here we describe the functional characterization of the <jats:italic>pleiades</jats:italic>, a cluster of ten effector genes, by analyzing the micro- and macroscopic phenotype of the cluster deletion and expressing these proteins <jats:italic>in planta</jats:italic>. Deletion of the <jats:italic>pleiades</jats:italic> leads to strongly impaired virulence and accumulation of reactive oxygen species (ROS) in infected tissue. Eight of the Pleiades suppress the production of ROS upon perception of pathogen associated molecular patterns (PAMPs). Although functionally redundant, the Pleiades target different host components. The paralogs Taygeta1 and Merope1 suppress ROS production in either the cytoplasm or nucleus, respectively. Merope1 targets and promotes the auto-ubiquitination activity of RFI2, a conserved family of E3 ligases that regulates the production of PAMP-triggered ROS burst in plants.","lang":"eng"}],"ddc":["580"],"day":"24"},{"external_id":{"isi":["000699841100001"],"pmid":["34578434"]},"author":[{"id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","full_name":"Obr, Martin","first_name":"Martin","last_name":"Obr","orcid":"0000-0003-1756-6564"},{"orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","first_name":"Florian KM","last_name":"Schur"},{"last_name":"Dick","full_name":"Dick, Robert A.","first_name":"Robert A."}],"title":"A structural perspective of the role of IP6 in immature and mature retroviral assembly","department":[{"_id":"FlSc"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"file":[{"creator":"cchlebak","file_id":"10115","checksum":"bcfd72a12977d48e22df3d0cc55aacf1","date_created":"2021-10-08T10:38:15Z","access_level":"open_access","relation":"main_file","date_updated":"2021-10-08T10:38:15Z","file_name":"2021_Viruses_Obr.pdf","success":1,"content_type":"application/pdf","file_size":4146796}],"scopus_import":"1","publication_status":"published","corr_author":"1","has_accepted_license":"1","article_number":"1853","oa_version":"Published Version","project":[{"name":"Structural conservation and diversity in retroviral capsid","call_identifier":"FWF","_id":"26736D6A-B435-11E9-9278-68D0E5697425","grant_number":"P31445"}],"day":"17","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"}],"ddc":["616"],"issue":"9","publication":"Viruses","date_created":"2021-10-07T09:13:29Z","quality_controlled":"1","publication_identifier":{"issn":["1999-4915"]},"language":[{"iso":"eng"}],"date_published":"2021-09-17T00:00:00Z","file_date_updated":"2021-10-08T10:38:15Z","citation":{"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.","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>","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.","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>.","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>","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>."},"month":"09","article_processing_charge":"Yes","volume":13,"oa":1,"intvolume":"        13","publisher":"MDPI","type":"journal_article","status":"public","keyword":["virology","infectious diseases"],"date_updated":"2025-04-15T08:24:49Z","doi":"10.3390/v13091853","acknowledgement":"We thank Volker M. Vogt for his critical comments in preparation of the review.","pmid":1,"year":"2021","_id":"10103","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_type":"original","isi":1}]