Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV
The crystal structure of the GP1–GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion. Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glyco...
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| Veröffentlicht in: | Nature structural & molecular biology 2016-06, Vol.23 (6), p.513-521 |
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| creator | Hastie, Kathryn M Igonet, Sébastien Sullivan, Brian M Legrand, Pierre Zandonatti, Michelle A Robinson, James E Garry, Robert F Rey, Félix A Oldstone, Michael B Saphire, Erica Ollmann |
| description | The crystal structure of the GP1–GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion.
Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1–GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1–GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states. |
| doi_str_mv | 10.1038/nsmb.3210 |
| format | Article |
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Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1–GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1–GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.3210</identifier><identifier>PMID: 27111888</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>13/106 ; 13/109 ; 13/31 ; 631/326/596/2116 ; 631/535/1266 ; 82/16 ; 82/80 ; 82/83 ; Animals ; Arenavirus ; Arenaviruses ; Biochemistry ; Biological Microscopy ; Cell Line ; Crystal structure ; Crystallography, X-Ray ; Crystals ; Drosophila ; Genetic aspects ; Glycoproteins ; Glycosylation ; Health aspects ; Humans ; Life Sciences ; Lymphocytic Choriomeningitis - metabolism ; Lymphocytic Choriomeningitis - virology ; Lymphocytic choriomeningitis virus - chemistry ; Lymphocytic choriomeningitis virus - physiology ; Membrane Biology ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - metabolism ; Models, Molecular ; Properties ; Protein Conformation ; Protein expression ; Protein Multimerization ; Protein Sorting Signals ; Protein Structure ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Structure ; Vaccines ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - metabolism ; Virulence (Microbiology) ; Virus Internalization ; Viruses</subject><ispartof>Nature structural & molecular biology, 2016-06, Vol.23 (6), p.513-521</ispartof><rights>Springer Nature America, Inc. 2016</rights><rights>COPYRIGHT 2016 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jun 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c739t-191d974eb4fdea0d4ca15c6739bb29fba4dcdebeeec4e2a4b79b9c167b5dae863</citedby><cites>FETCH-LOGICAL-c739t-191d974eb4fdea0d4ca15c6739bb29fba4dcdebeeec4e2a4b79b9c167b5dae863</cites><orcidid>0000-0003-2431-2255</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,781,785,886,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27111888$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hastie, Kathryn M</creatorcontrib><creatorcontrib>Igonet, Sébastien</creatorcontrib><creatorcontrib>Sullivan, Brian M</creatorcontrib><creatorcontrib>Legrand, Pierre</creatorcontrib><creatorcontrib>Zandonatti, Michelle A</creatorcontrib><creatorcontrib>Robinson, James E</creatorcontrib><creatorcontrib>Garry, Robert F</creatorcontrib><creatorcontrib>Rey, Félix A</creatorcontrib><creatorcontrib>Oldstone, Michael B</creatorcontrib><creatorcontrib>Saphire, Erica Ollmann</creatorcontrib><title>Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>The crystal structure of the GP1–GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion.
Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1–GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1–GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.</description><subject>13/106</subject><subject>13/109</subject><subject>13/31</subject><subject>631/326/596/2116</subject><subject>631/535/1266</subject><subject>82/16</subject><subject>82/80</subject><subject>82/83</subject><subject>Animals</subject><subject>Arenavirus</subject><subject>Arenaviruses</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Cell Line</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Drosophila</subject><subject>Genetic aspects</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Lymphocytic Choriomeningitis - metabolism</subject><subject>Lymphocytic Choriomeningitis - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hastie, Kathryn M</au><au>Igonet, Sébastien</au><au>Sullivan, Brian M</au><au>Legrand, Pierre</au><au>Zandonatti, Michelle A</au><au>Robinson, James E</au><au>Garry, Robert F</au><au>Rey, Félix A</au><au>Oldstone, Michael B</au><au>Saphire, Erica Ollmann</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2016-06-01</date><risdate>2016</risdate><volume>23</volume><issue>6</issue><spage>513</spage><epage>521</epage><pages>513-521</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>The crystal structure of the GP1–GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion.
Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1–GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1–GP2 complex of the prototypic arenavirus LCMV at 3.5 Å. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>27111888</pmid><doi>10.1038/nsmb.3210</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-2431-2255</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 13/106 13/109 13/31 631/326/596/2116 631/535/1266 82/16 82/80 82/83 Animals Arenavirus Arenaviruses Biochemistry Biological Microscopy Cell Line Crystal structure Crystallography, X-Ray Crystals Drosophila Genetic aspects Glycoproteins Glycosylation Health aspects Humans Life Sciences Lymphocytic Choriomeningitis - metabolism Lymphocytic Choriomeningitis - virology Lymphocytic choriomeningitis virus - chemistry Lymphocytic choriomeningitis virus - physiology Membrane Biology Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Models, Molecular Properties Protein Conformation Protein expression Protein Multimerization Protein Sorting Signals Protein Structure Protein Subunits - chemistry Protein Subunits - metabolism Structure Vaccines Viral Envelope Proteins - chemistry Viral Envelope Proteins - metabolism Virulence (Microbiology) Virus Internalization Viruses |
| title | Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV |
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