Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited
Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibri...
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| creator | Roche, S Albertini, A. A. V Lepault, J Bressanelli, S Gaudin, Y |
| description | Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins. Comparison of the structures of G pre- and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins. |
| doi_str_mv | 10.1007/s00018-008-7534-3 |
| format | Article |
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A. V ; Lepault, J ; Bressanelli, S ; Gaudin, Y</creator><creatorcontrib>Roche, S ; Albertini, A. A. V ; Lepault, J ; Bressanelli, S ; Gaudin, Y</creatorcontrib><description>Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins. Comparison of the structures of G pre- and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-008-7534-3</identifier><identifier>PMID: 18345480</identifier><language>eng</language><publisher>Basel: Basel : SP Birkhäuser Verlag Basel</publisher><subject>Amino Acid Sequence ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Cellular biology ; conformational change ; Endocytosis ; glycoprotein ; Hydrogen-Ion Concentration ; Life Sciences ; membrane fusion ; Membrane Fusion - physiology ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Membranes ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Paramyxovirus ; Protein Conformation ; Proteins ; Respirovirus ; Review ; Rhabdoviridae - metabolism ; rhabdovirus ; Vesicular stomatitis Indiana virus - metabolism ; Vesicular stomatitis virus ; Vesiculovirus ; viral entry ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - metabolism ; Virus Internalization ; Viruses</subject><ispartof>Cellular and molecular life sciences : CMLS, 2008-06, Vol.65 (11), p.1716-1728</ispartof><rights>Birkhaueser 2008</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c623t-7c2c31d7852889de1ff1c2585be29e90e21b75a92415c1cb6a7a5a6ab8582923</citedby><orcidid>0000-0002-2076-1654</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131878/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131878/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,725,778,782,883,27907,27908,41471,42540,51302,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18345480$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02660923$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Roche, S</creatorcontrib><creatorcontrib>Albertini, A. A. V</creatorcontrib><creatorcontrib>Lepault, J</creatorcontrib><creatorcontrib>Bressanelli, S</creatorcontrib><creatorcontrib>Gaudin, Y</creatorcontrib><title>Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins. Comparison of the structures of G pre- and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Cellular biology</subject><subject>conformational change</subject><subject>Endocytosis</subject><subject>glycoprotein</subject><subject>Hydrogen-Ion Concentration</subject><subject>Life Sciences</subject><subject>membrane fusion</subject><subject>Membrane Fusion - physiology</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membranes</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Paramyxovirus</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Respirovirus</subject><subject>Review</subject><subject>Rhabdoviridae - metabolism</subject><subject>rhabdovirus</subject><subject>Vesicular stomatitis Indiana virus - metabolism</subject><subject>Vesicular stomatitis virus</subject><subject>Vesiculovirus</subject><subject>viral entry</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Virus Internalization</subject><subject>Viruses</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkktv1DAUhSMEog_4AWwg6gKJReBeO36ETVVVpUUaCaQWiZ3leJypqyQebCdS_z0eZURLF7Cy5fudc-3rUxRvED4igPgUAQBlBSArwWhd0WfFIdYEqgYEPt_vuSQ_D4qjGO8yzCThL4sDlLRmtYTD4vt1CpNJU7Cx9F052-jM1OtQxuQHnVxysZxdmGK56e-N3wafrBs_l4Md2qBHW3ZTdH4sg51ddMmuXxUvOt1H-3q_Hhc3Xy5uzq-q1bfLr-dnq8pwQlMlDDEU10IyImWztth1aAiTrLWksQ1Ygq1guiE1MoOm5VpoprluZX5CQ-hxcbrYbqd2sGtjxxR0r7bBDTrcK6-d-rsyulu18bNCRIpSyOzwYXG4faK7Olup3RkQziG3mjGz7_fdgv812ZjU4KKxfZ8n4KeoBPIahfw_SEAKISjP4MkT8M5PYcwTUwQpQ-RyB-ECmeBjDLb7c08EtUuAWhKgcgLULgGKZs3bx4N5UOy_PANkAWIujRsbHjr_y_XdIuq0V3oTXFQ_rgkgBWiAsprR39X2xVw</recordid><startdate>20080601</startdate><enddate>20080601</enddate><creator>Roche, S</creator><creator>Albertini, A. 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A. V</au><au>Lepault, J</au><au>Bressanelli, S</au><au>Gaudin, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2008-06-01</date><risdate>2008</risdate><volume>65</volume><issue>11</issue><spage>1716</spage><epage>1728</epage><pages>1716-1728</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins. Comparison of the structures of G pre- and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins.</abstract><cop>Basel</cop><pub>Basel : SP Birkhäuser Verlag Basel</pub><pmid>18345480</pmid><doi>10.1007/s00018-008-7534-3</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-2076-1654</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Cellular biology conformational change Endocytosis glycoprotein Hydrogen-Ion Concentration Life Sciences membrane fusion Membrane Fusion - physiology Membrane Glycoproteins - chemistry Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Membranes Models, Molecular Molecular Sequence Data Mutation Paramyxovirus Protein Conformation Proteins Respirovirus Review Rhabdoviridae - metabolism rhabdovirus Vesicular stomatitis Indiana virus - metabolism Vesicular stomatitis virus Vesiculovirus viral entry Viral Envelope Proteins - chemistry Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Virus Internalization Viruses |
| title | Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited |
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