A structural analysis of M protein in coronavirus assembly and morphology
The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, t...
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| Veröffentlicht in: | Journal of structural biology 2011-04, Vol.174 (1), p.11-22 |
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| container_title | Journal of structural biology |
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| creator | Neuman, Benjamin W. Kiss, Gabriella Kunding, Andreas H. Bhella, David Baksh, M. Fazil Connelly, Stephen Droese, Ben Klaus, Joseph P. Makino, Shinji Sawicki, Stanley G. Siddell, Stuart G. Stamou, Dimitrios G. Wilson, Ian A. Kuhn, Peter Buchmeier, Michael J. |
| description | The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly. |
| doi_str_mv | 10.1016/j.jsb.2010.11.021 |
| format | Article |
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Fazil ; Connelly, Stephen ; Droese, Ben ; Klaus, Joseph P. ; Makino, Shinji ; Sawicki, Stanley G. ; Siddell, Stuart G. ; Stamou, Dimitrios G. ; Wilson, Ian A. ; Kuhn, Peter ; Buchmeier, Michael J.</creator><creatorcontrib>Neuman, Benjamin W. ; Kiss, Gabriella ; Kunding, Andreas H. ; Bhella, David ; Baksh, M. Fazil ; Connelly, Stephen ; Droese, Ben ; Klaus, Joseph P. ; Makino, Shinji ; Sawicki, Stanley G. ; Siddell, Stuart G. ; Stamou, Dimitrios G. ; Wilson, Ian A. ; Kuhn, Peter ; Buchmeier, Michael J.</creatorcontrib><description>The M protein of coronavirus plays a central role in virus assembly, turning cellular membranes into workshops where virus and host factors come together to make new virus particles. We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.</description><identifier>ISSN: 1047-8477</identifier><identifier>EISSN: 1095-8657</identifier><identifier>DOI: 10.1016/j.jsb.2010.11.021</identifier><identifier>PMID: 21130884</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cell Line ; Coronavirus ; Coronavirus - metabolism ; Coronavirus - ultrastructure ; Coronavirus M Proteins ; Cryo-electron microscopy ; Cryo-electron tomography ; Cryoelectron Microscopy ; Electron Microscope Tomography ; Humans ; Pleomorphic virus structure ; Viral matrix protein ; Viral Matrix Proteins - ultrastructure ; Virus Assembly - physiology ; Virus Assembly - radiation effects</subject><ispartof>Journal of structural biology, 2011-04, Vol.174 (1), p.11-22</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved. 2010 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-81fce937d791f8790cbc4407e07e05725f2b3744a746e260676b52eb17e0f8023</citedby><cites>FETCH-LOGICAL-c516t-81fce937d791f8790cbc4407e07e05725f2b3744a746e260676b52eb17e0f8023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1047847710003588$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21130884$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Neuman, Benjamin W.</creatorcontrib><creatorcontrib>Kiss, Gabriella</creatorcontrib><creatorcontrib>Kunding, Andreas H.</creatorcontrib><creatorcontrib>Bhella, David</creatorcontrib><creatorcontrib>Baksh, M. 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We investigated how M structure and organization is related to virus shape and size using cryo-electron microscopy, tomography and statistical analysis. We present evidence that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer. Elongated M protein is associated with rigidity, clusters of spikes and a relatively narrow range of membrane curvature. In contrast, compact M protein is associated with flexibility and low spike density. Analysis of several types of virus-like particles and virions revealed that S protein, N protein and genomic RNA each help to regulate virion size and variation, presumably through interactions with M. These findings provide insight into how M protein functions to promote virus assembly.</description><subject>Cell Line</subject><subject>Coronavirus</subject><subject>Coronavirus - metabolism</subject><subject>Coronavirus - ultrastructure</subject><subject>Coronavirus M Proteins</subject><subject>Cryo-electron microscopy</subject><subject>Cryo-electron tomography</subject><subject>Cryoelectron Microscopy</subject><subject>Electron Microscope Tomography</subject><subject>Humans</subject><subject>Pleomorphic virus structure</subject><subject>Viral matrix protein</subject><subject>Viral Matrix Proteins - ultrastructure</subject><subject>Virus Assembly - physiology</subject><subject>Virus Assembly - radiation effects</subject><issn>1047-8477</issn><issn>1095-8657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1LxDAQhoMo7vrxA7xIb566ZtK0ySIIIn4sKF70HNJ0qlnaZk3ahf33pqwuehEGZsI882aYl5AzoDOgUFwuZ8tQzhgd3zCjDPbIFOg8T2WRi_2x5iKVXIgJOQphSSnlwOCQTBhARqXkU7K4SULvB9MPXjeJ7nSzCTYkrk6ek5V3PdouiWGcd51eWz-ERIeAbdlsIl0lrfOrD9e4980JOah1E_D0Ox-Tt_u719vH9OnlYXF785SaHIo-lVAbnGeiEnOopZhTUxrOqcAxcsHympWZ4FwLXiAraCGKMmdYQmzXkrLsmFxvdVdD2WJlsOvj6mrlbav9Rjlt1d9OZz_Uu1srzmWUgyhw8S3g3eeAoVetDQabRnfohqBkLoAxluWRhC1pvAvBY737BagaHVBLFR1QowMKQEUH4sz57_V2Ez8nj8DVFsB4pLVFr4Kx2BmsrEfTq8rZf-S_AGsRl0c</recordid><startdate>20110401</startdate><enddate>20110401</enddate><creator>Neuman, Benjamin W.</creator><creator>Kiss, Gabriella</creator><creator>Kunding, Andreas H.</creator><creator>Bhella, David</creator><creator>Baksh, M. 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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Cell Line Coronavirus Coronavirus - metabolism Coronavirus - ultrastructure Coronavirus M Proteins Cryo-electron microscopy Cryo-electron tomography Cryoelectron Microscopy Electron Microscope Tomography Humans Pleomorphic virus structure Viral matrix protein Viral Matrix Proteins - ultrastructure Virus Assembly - physiology Virus Assembly - radiation effects |
| title | A structural analysis of M protein in coronavirus assembly and morphology |
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