[{"publication_identifier":{"issn":["0022-538X"],"eissn":["1098-5514"]},"month":"03","keyword":["virology","insect science","immunology","microbiology"],"title":"The Orthobunyavirus Germiston enters host cells from late endosomes","ddc":["570"],"project":[{"call_identifier":"FWF","_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid","grant_number":"P31445"}],"volume":96,"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."}],"type":"journal_article","fulldoi":"https://doi.org/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.","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8906410","open_access":"1"}],"doi":"10.1128/jvi.02146-21","date_created":"2022-01-18T10:04:18Z","author":[{"last_name":"Windhaber","first_name":"Stefan","full_name":"Windhaber, Stefan"},{"first_name":"Qilin","full_name":"Xin, Qilin","last_name":"Xin"},{"full_name":"Uckeley, Zina M.","first_name":"Zina M.","last_name":"Uckeley"},{"full_name":"Koch, Jana","first_name":"Jana","last_name":"Koch"},{"orcid":"0000-0003-1756-6564","full_name":"Obr, Martin","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","last_name":"Obr"},{"last_name":"Garnier","full_name":"Garnier, Céline","first_name":"Céline"},{"last_name":"Luengo-Guyonnot","full_name":"Luengo-Guyonnot, Catherine","first_name":"Catherine"},{"first_name":"Maëva","full_name":"Duboeuf, Maëva","last_name":"Duboeuf"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian KM","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","last_name":"Schur"},{"last_name":"Lozach","full_name":"Lozach, Pierre-Yves","first_name":"Pierre-Yves"}],"department":[{"_id":"FlSc"}],"intvolume":"        96","date_updated":"2026-06-18T08:44:25Z","publisher":"American Society for Microbiology","external_id":{"pmid":["35019710"],"isi":["000779305000033"]},"issue":"5","isi":1,"publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","day":"01","publication":"Journal of Virology","article_number":"e02146-21","quality_controlled":"1","status":"public","_id":"10639","citation":{"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.","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>","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>","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>.","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.","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>.","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)."},"scopus_import":"1","oa":1,"date_published":"2022-03-01T00:00:00Z","year":"2022","language":[{"iso":"eng"}],"pmid":1,"acknowledged_ssus":[{"_id":"EM-Fac"}],"oa_version":"Published Version","article_processing_charge":"No"},{"month":"05","title":"Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging","extern":"1","publication_identifier":{"issn":["0022-538X"],"eissn":["1098-5514"]},"DOAJ_listed":"1","publist_id":"6835","volume":90,"abstract":[{"text":"The Gag polyprotein of retroviruses drives immature virus assembly by forming hexameric protein lattices. The assembly is primarily mediated by protein-protein interactions between capsid (CA) domains and by interactions between nucleocapsid (NC) domains and RNA. Specific interactions between NC and the viral RNA are required for genome packaging. Previously reported cryoelectron microscopy analysis of immature Mason-Pfizer monkey virus (M-PMV) particles suggested that a basic region (residues RKK) in CA may serve as an additional binding site for nucleic acids. Here, we have introduced mutations into the RKK region in both bacterial and proviral M-PMV vectors and have assessed their impact on M-PMV assembly, structure, RNA binding, budding/release, nuclear trafficking, and infectivity using in vitro and in vivo systems. Our data indicate that the RKK region binds and structures nucleic acid that serves to promote virus particle assembly in the cytoplasm. Moreover, the RKK region appears to be important for recruitment of viral genomic RNA into Gag particles, and this function could be linked to changes in nuclear trafficking. Together these observations suggest that in M-PMV, direct interactions between CA and nucleic acid play important functions in the late stages of the viral life cycle.","lang":"eng"}],"fulldoi":"https://doi.org/10.1128/JVI.03197-15","type":"journal_article","doi":"10.1128/JVI.03197-15","main_file_link":[{"url":"https://doi.org/10.1128/jvi.03197-15","open_access":"1"}],"acknowledgement":"Work in the laboratory of John A. G. Briggs was funded by Deutsche\r\nForschungsgemeinschaft (DFG) (BR 3635/2-1). This work, including the\r\nefforts of Tomas Ruml, was funded by the Grant Agency of the Czech\r\nRepublic (14-15326S) and the Czech Ministry of Education (NPU I sus-\r\ntainability projects LO1302 and LO1304).","page":"4593 - 4603","publisher":"American Society for Microbiology","author":[{"last_name":"Füzik","first_name":"Tibor","full_name":"Füzik, Tibor"},{"last_name":"Píchalová","first_name":"Růžena","full_name":"Píchalová, Růžena"},{"first_name":"Florian","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian","last_name":"Schur"},{"last_name":"Strohalmová","first_name":"Karolína","full_name":"Strohalmová, Karolína"},{"last_name":"Křížová","first_name":"Ivana","full_name":"Křížová, Ivana"},{"full_name":"Hadravová, Romana","first_name":"Romana","last_name":"Hadravová"},{"full_name":"Rumlová, Michaela","first_name":"Michaela","last_name":"Rumlová"},{"first_name":"John","full_name":"Briggs, John","last_name":"Briggs"},{"first_name":"Pavel","full_name":"Ulbrich, Pavel","last_name":"Ulbrich"},{"last_name":"Ruml","first_name":"Tomáš","full_name":"Ruml, Tomáš"}],"date_created":"2018-12-11T11:48:38Z","OA_type":"gold","date_updated":"2026-05-20T07:34:00Z","intvolume":"        90","external_id":{"pmid":["26912613"]},"issue":"9","publication_status":"published","OA_place":"publisher","day":"01","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","article_type":"original","publication":"Journal of Virology","_id":"813","citation":{"ista":"Füzik T, Píchalová R, Schur FK, Strohalmová K, Křížová I, Hadravová R, Rumlová M, Briggs J, Ulbrich P, Ruml T. 2016. Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging. Journal of Virology. 90(9), 4593–4603.","apa":"Füzik, T., Píchalová, R., Schur, F. K., Strohalmová, K., Křížová, I., Hadravová, R., … Ruml, T. (2016). Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging. <i>Journal of Virology</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/JVI.03197-15\">https://doi.org/10.1128/JVI.03197-15</a>","ama":"Füzik T, Píchalová R, Schur FK, et al. Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging. <i>Journal of Virology</i>. 2016;90(9):4593-4603. doi:<a href=\"https://doi.org/10.1128/JVI.03197-15\">10.1128/JVI.03197-15</a>","mla":"Füzik, Tibor, et al. “Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging.” <i>Journal of Virology</i>, vol. 90, no. 9, American Society for Microbiology, 2016, pp. 4593–603, doi:<a href=\"https://doi.org/10.1128/JVI.03197-15\">10.1128/JVI.03197-15</a>.","ieee":"T. Füzik <i>et al.</i>, “Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging,” <i>Journal of Virology</i>, vol. 90, no. 9. American Society for Microbiology, pp. 4593–4603, 2016.","chicago":"Füzik, Tibor, Růžena Píchalová, Florian KM Schur, Karolína Strohalmová, Ivana Křížová, Romana Hadravová, Michaela Rumlová, John Briggs, Pavel Ulbrich, and Tomáš Ruml. “Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging.” <i>Journal of Virology</i>. American Society for Microbiology, 2016. <a href=\"https://doi.org/10.1128/JVI.03197-15\">https://doi.org/10.1128/JVI.03197-15</a>.","short":"T. Füzik, R. Píchalová, F.K. Schur, K. Strohalmová, I. Křížová, R. Hadravová, M. Rumlová, J. Briggs, P. Ulbrich, T. Ruml, Journal of Virology 90 (2016) 4593–4603."},"quality_controlled":"1","status":"public","scopus_import":"1","oa":1,"year":"2016","date_published":"2016-05-01T00:00:00Z","language":[{"iso":"eng"}],"pmid":1,"oa_version":"Published Version","article_processing_charge":"No"},{"oa_version":"Published Version","article_processing_charge":"No","year":"2015","date_published":"2015-09-22T00:00:00Z","language":[{"iso":"eng"}],"pmid":1,"oa":1,"scopus_import":"1","tmp":{"image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"quality_controlled":"1","status":"public","_id":"815","citation":{"chicago":"Schur, Florian KM, Robert Dick, Wim Hagen, Volker Vogt, and John Briggs. “The Structure of Immature Virus like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the P10 Domain in Assembly.” <i>Journal of Virology</i>. ASM, 2015. <a href=\"https://doi.org/10.1128/JVI.01502-15\">https://doi.org/10.1128/JVI.01502-15</a>.","ieee":"F. K. Schur, R. Dick, W. Hagen, V. Vogt, and J. Briggs, “The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly,” <i>Journal of Virology</i>, vol. 89, no. 20. ASM, pp. 10294–10302, 2015.","short":"F.K. Schur, R. Dick, W. Hagen, V. Vogt, J. Briggs, Journal of Virology 89 (2015) 10294–10302.","ista":"Schur FK, Dick R, Hagen W, Vogt V, Briggs J. 2015. The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. Journal of Virology. 89(20), 10294–10302.","apa":"Schur, F. K., Dick, R., Hagen, W., Vogt, V., &#38; Briggs, J. (2015). The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. <i>Journal of Virology</i>. ASM. <a href=\"https://doi.org/10.1128/JVI.01502-15\">https://doi.org/10.1128/JVI.01502-15</a>","ama":"Schur FK, Dick R, Hagen W, Vogt V, Briggs J. The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. <i>Journal of Virology</i>. 2015;89(20):10294-10302. doi:<a href=\"https://doi.org/10.1128/JVI.01502-15\">10.1128/JVI.01502-15</a>","mla":"Schur, Florian KM, et al. “The Structure of Immature Virus like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the P10 Domain in Assembly.” <i>Journal of Virology</i>, vol. 89, no. 20, ASM, 2015, pp. 10294–302, doi:<a href=\"https://doi.org/10.1128/JVI.01502-15\">10.1128/JVI.01502-15</a>."},"publication":"Journal of Virology","article_type":"original","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","day":"22","OA_place":"publisher","publication_status":"published","external_id":{"pmid":["26223638"]},"issue":"20","OA_type":"gold","author":[{"first_name":"Florian","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian","orcid":"0000-0003-4790-8078","last_name":"Schur"},{"first_name":"Robert","full_name":"Dick, Robert","last_name":"Dick"},{"first_name":"Wim","full_name":"Hagen, Wim","last_name":"Hagen"},{"full_name":"Vogt, Volker","first_name":"Volker","last_name":"Vogt"},{"last_name":"Briggs","first_name":"John","full_name":"Briggs, John"}],"date_created":"2018-12-11T11:48:39Z","intvolume":"        89","date_updated":"2026-05-18T12:47:51Z","page":"10294 - 10302","publisher":"ASM","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1128/jvi.01502-15"}],"doi":"10.1128/JVI.01502-15","abstract":[{"lang":"eng","text":"The polyprotein Gag is the primary structural component of retroviruses. Gag consists of independently folded domains connected by flexible linkers. Interactions between the conserved capsid (CA) domains of Gag mediate formation of hexameric protein lattices that drive assembly of immature virus particles. Proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Within the assembled Gag lattices of HIV-1 and Mason- Pfizer monkey virus (M-PMV), the C-terminal domain of CA adopts similar quaternary arrangements, while the N-terminal domain of CA is packed in very different manners. Here, we have used cryo-electron tomography and subtomogram averaging to study in vitro-assembled, immature virus-like Rous sarcoma virus (RSV) Gag particles and have determined the structure of CA and the surrounding regions to a resolution of ~8 Å. We found that the C-terminal domain of RSV CA is arranged similarly to HIV-1 and M-PMV, whereas the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears to be inaccessible to PR. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. We have also assessed the affect of lattice assembly on proteolytic processing by exogenous PR. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, a finding consistent with structural regulation of proteolytic maturation.\r\n"}],"volume":89,"type":"journal_article","fulldoi":"https://doi.org/10.1128/JVI.01502-15","publist_id":"6837","DOAJ_listed":"1","license":"https://creativecommons.org/licenses/by/4.0/","extern":"1","publication_identifier":{"eissn":["1098-5514"],"issn":["0022-538X"]},"month":"09","title":"The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly"},{"file":[{"file_name":"IST-2016-417-v1+1_J._Virol.-2014-Kuchibhatla-10-20.pdf","relation":"main_file","access_level":"open_access","date_updated":"2020-07-14T12:45:34Z","content_type":"application/pdf","date_created":"2018-12-12T10:13:43Z","file_size":825756,"file_id":"5029","checksum":"2c121b5e884992dfec5605bdf4e659da","creator":"system"}],"type":"journal_article","fulldoi":"https://doi.org/10.1128/JVI.02595-13","abstract":[{"text":"The genome sequences of new viruses often contain many &quot;orphan&quot; or &quot;taxon-specific&quot; proteins apparently lacking homologs. However, because viral proteins evolve very fast, commonly used sequence similarity detection methods such as BLAST may overlook homologs. We analyzed a data set of proteins from RNA viruses characterized as &quot;genus specific&quot; by BLAST. More powerful methods developed recently, such as HHblits or HHpred (available through web-based, user-friendly interfaces), could detect distant homologs of a quarter of these proteins, suggesting that these methods should be used to annotate viral genomes. In-depth manual analyses of a subset of the remaining sequences, guided by contextual information such as taxonomy, gene order, or domain cooccurrence, identified distant homologs of another third. Thus, a combination of powerful automated methods and manual analyses can uncover distant homologs of many proteins thought to be orphans. We expect these methodological results to be also applicable to cellular organisms, since they generally evolve much more slowly than RNA viruses. As an application, we reanalyzed the genome of a bee pathogen, Chronic bee paralysis virus (CBPV). We could identify homologs of most of its proteins thought to be orphans; in each case, identifying homologs provided functional clues. We discovered that CBPV encodes a domain homologous to the Alphavirus methyltransferase-guanylyltransferase; a putative membrane protein, SP24, with homologs in unrelated insect viruses and insect-transmitted plant viruses having different morphologies (cileviruses, higreviruses, blunerviruses, negeviruses); and a putative virion glycoprotein, ORF2, also found in negeviruses. SP24 and ORF2 are probably major structural components of the virionsd.","lang":"eng"}],"volume":88,"publication_identifier":{"issn":["0022-538X"]},"license":"https://creativecommons.org/licenses/by/3.0/","title":"Powerful sequence similarity search methods and in-depth manual analyses can identify remote homologs in many apparently \"orphan\" viral proteins","month":"01","publist_id":"4698","ddc":["570"],"issue":"1","external_id":{"isi":["000329194600002"]},"isi":1,"publication_status":"published","doi":"10.1128/JVI.02595-13","intvolume":"        88","department":[{"_id":"MD"}],"date_updated":"2026-07-28T10:18:04Z","date_created":"2018-12-11T11:56:34Z","author":[{"last_name":"Kuchibhatla","first_name":"Durga","full_name":"Kuchibhatla, Durga"},{"last_name":"Sherman","first_name":"Westley","full_name":"Sherman, Westley"},{"full_name":"Chung, Betty","first_name":"Betty","last_name":"Chung"},{"last_name":"Cook","first_name":"Shelley","full_name":"Cook, Shelley"},{"full_name":"Schneider, Georg","first_name":"Georg","id":"329095A0-F248-11E8-B48F-1D18A9856A87","last_name":"Schneider"},{"last_name":"Eisenhaber","full_name":"Eisenhaber, Birgit","first_name":"Birgit"},{"last_name":"Karlin","first_name":"David","full_name":"Karlin, David"}],"publisher":"ASM","page":"10 - 20","status":"public","quality_controlled":"1","citation":{"ama":"Kuchibhatla D, Sherman W, Chung B, et al. Powerful sequence similarity search methods and in-depth manual analyses can identify remote homologs in many apparently “orphan” viral proteins. <i>Journal of Virology</i>. 2014;88(1):10-20. doi:<a href=\"https://doi.org/10.1128/JVI.02595-13\">10.1128/JVI.02595-13</a>","ista":"Kuchibhatla D, Sherman W, Chung B, Cook S, Schneider G, Eisenhaber B, Karlin D. 2014. Powerful sequence similarity search methods and in-depth manual analyses can identify remote homologs in many apparently ‘orphan’ viral proteins. Journal of Virology. 88(1), 10–20.","apa":"Kuchibhatla, D., Sherman, W., Chung, B., Cook, S., Schneider, G., Eisenhaber, B., &#38; Karlin, D. (2014). Powerful sequence similarity search methods and in-depth manual analyses can identify remote homologs in many apparently “orphan” viral proteins. <i>Journal of Virology</i>. ASM. <a href=\"https://doi.org/10.1128/JVI.02595-13\">https://doi.org/10.1128/JVI.02595-13</a>","mla":"Kuchibhatla, Durga, et al. “Powerful Sequence Similarity Search Methods and In-Depth Manual Analyses Can Identify Remote Homologs in Many Apparently ‘Orphan’ Viral Proteins.” <i>Journal of Virology</i>, vol. 88, no. 1, ASM, 2014, pp. 10–20, doi:<a href=\"https://doi.org/10.1128/JVI.02595-13\">10.1128/JVI.02595-13</a>.","chicago":"Kuchibhatla, Durga, Westley Sherman, Betty Chung, Shelley Cook, Georg Schneider, Birgit Eisenhaber, and David Karlin. “Powerful Sequence Similarity Search Methods and In-Depth Manual Analyses Can Identify Remote Homologs in Many Apparently ‘Orphan’ Viral Proteins.” <i>Journal of Virology</i>. ASM, 2014. <a href=\"https://doi.org/10.1128/JVI.02595-13\">https://doi.org/10.1128/JVI.02595-13</a>.","ieee":"D. Kuchibhatla <i>et al.</i>, “Powerful sequence similarity search methods and in-depth manual analyses can identify remote homologs in many apparently ‘orphan’ viral proteins,” <i>Journal of Virology</i>, vol. 88, no. 1. ASM, pp. 10–20, 2014.","short":"D. Kuchibhatla, W. Sherman, B. Chung, S. Cook, G. Schneider, B. Eisenhaber, D. Karlin, Journal of Virology 88 (2014) 10–20."},"_id":"2250","scopus_import":"1","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)","short":"CC BY (3.0)"},"pubrep_id":"417","day":"01","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Journal of Virology","has_accepted_license":"1","file_date_updated":"2020-07-14T12:45:34Z","article_processing_charge":"No","das_tickbox":"1","oa_version":"Published Version","oa":1,"language":[{"iso":"eng"}],"date_published":"2014-01-01T00:00:00Z","year":"2014"}]