Structure of the hepatitis C virus E1E2 glycoprotein complex
Hepatitis C virus (HCV) infection is a leading cause of chronic liver disease, cirrhosis, and hepatocellular carcinoma in humans and afflicts more than 58 million people worldwide. The HCV envelope E1 and E2 glycoproteins are essential for viral entry and comprise the primary antigenic target for ne...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2022-10, Vol.378 (6617), p.263-269 |
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| creator | Torrents de la Peña, Alba Sliepen, Kwinten Eshun-Wilson, Lisa Newby, Maddy L Allen, Joel D Zon, Ian Koekkoek, Sylvie Chumbe, Ana Crispin, Max Schinkel, Janke Lander, Gabriel C Sanders, Rogier W Ward, Andrew B |
| description | Hepatitis C virus (HCV) infection is a leading cause of chronic liver disease, cirrhosis, and hepatocellular carcinoma in humans and afflicts more than 58 million people worldwide. The HCV envelope E1 and E2 glycoproteins are essential for viral entry and comprise the primary antigenic target for neutralizing antibody responses. The molecular mechanisms of E1E2 assembly, as well as how the E1E2 heterodimer binds broadly neutralizing antibodies, remain elusive. Here, we present the cryo-electron microscopy structure of the membrane-extracted full-length E1E2 heterodimer in complex with three broadly neutralizing antibodies-AR4A, AT1209, and IGH505-at ~3.5-angstrom resolution. We resolve the interface between the E1 and E2 ectodomains and deliver a blueprint for the rational design of vaccine immunogens and antiviral drugs. |
| doi_str_mv | 10.1126/science.abn9884 |
| format | Article |
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The HCV envelope E1 and E2 glycoproteins are essential for viral entry and comprise the primary antigenic target for neutralizing antibody responses. The molecular mechanisms of E1E2 assembly, as well as how the E1E2 heterodimer binds broadly neutralizing antibodies, remain elusive. Here, we present the cryo-electron microscopy structure of the membrane-extracted full-length E1E2 heterodimer in complex with three broadly neutralizing antibodies-AR4A, AT1209, and IGH505-at ~3.5-angstrom resolution. We resolve the interface between the E1 and E2 ectodomains and deliver a blueprint for the rational design of vaccine immunogens and antiviral drugs.</description><identifier>ISSN: 0036-8075</identifier><identifier>ISSN: 1095-9203</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.abn9884</identifier><identifier>PMID: 36264808</identifier><language>eng</language><publisher>United States: The American Association for the Advancement of Science</publisher><subject>Antibodies ; Antiviral Agents - chemistry ; Broadly Neutralizing Antibodies ; Cancer vaccines ; Chronic infection ; Cirrhosis ; Cryoelectron Microscopy ; Drug development ; Electron microscopy ; Epitopes ; Glycoproteins ; Hepacivirus - chemistry ; Hepacivirus - immunology ; Hepatitis ; Hepatitis C ; Hepatitis C - virology ; Humans ; Liver ; Liver cancer ; Liver cirrhosis ; Neutralizing ; Protein Multimerization ; Torrents ; Vaccine development ; Vaccines ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - immunology ; Viral Hepatitis Vaccines - chemistry ; Viral Hepatitis Vaccines - immunology ; Viruses</subject><ispartof>Science (American Association for the Advancement of Science), 2022-10, Vol.378 (6617), p.263-269</ispartof><rights>Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-55c72ceaae629245be7b2429c03b328eb68590305019fba88893b6f670307a383</citedby><cites>FETCH-LOGICAL-c422t-55c72ceaae629245be7b2429c03b328eb68590305019fba88893b6f670307a383</cites><orcidid>0000-0001-6988-1457 ; 0000-0002-1072-2694 ; 0000-0003-0624-245X ; 0000-0003-2547-968X ; 0000-0001-5598-1780 ; 0000-0003-0870-5075 ; 0000-0002-2324-8573 ; 0000-0001-7153-3769 ; 0000-0003-4346-0739 ; 0000-0003-4921-1135 ; 0000-0003-1414-0648</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,2871,2872,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36264808$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Torrents de la Peña, Alba</creatorcontrib><creatorcontrib>Sliepen, Kwinten</creatorcontrib><creatorcontrib>Eshun-Wilson, Lisa</creatorcontrib><creatorcontrib>Newby, Maddy L</creatorcontrib><creatorcontrib>Allen, Joel D</creatorcontrib><creatorcontrib>Zon, Ian</creatorcontrib><creatorcontrib>Koekkoek, Sylvie</creatorcontrib><creatorcontrib>Chumbe, Ana</creatorcontrib><creatorcontrib>Crispin, Max</creatorcontrib><creatorcontrib>Schinkel, Janke</creatorcontrib><creatorcontrib>Lander, Gabriel C</creatorcontrib><creatorcontrib>Sanders, Rogier W</creatorcontrib><creatorcontrib>Ward, Andrew B</creatorcontrib><title>Structure of the hepatitis C virus E1E2 glycoprotein complex</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Hepatitis C virus (HCV) infection is a leading cause of chronic liver disease, cirrhosis, and hepatocellular carcinoma in humans and afflicts more than 58 million people worldwide. The HCV envelope E1 and E2 glycoproteins are essential for viral entry and comprise the primary antigenic target for neutralizing antibody responses. The molecular mechanisms of E1E2 assembly, as well as how the E1E2 heterodimer binds broadly neutralizing antibodies, remain elusive. Here, we present the cryo-electron microscopy structure of the membrane-extracted full-length E1E2 heterodimer in complex with three broadly neutralizing antibodies-AR4A, AT1209, and IGH505-at ~3.5-angstrom resolution. We resolve the interface between the E1 and E2 ectodomains and deliver a blueprint for the rational design of vaccine immunogens and antiviral drugs.</description><subject>Antibodies</subject><subject>Antiviral Agents - chemistry</subject><subject>Broadly Neutralizing Antibodies</subject><subject>Cancer vaccines</subject><subject>Chronic infection</subject><subject>Cirrhosis</subject><subject>Cryoelectron Microscopy</subject><subject>Drug development</subject><subject>Electron microscopy</subject><subject>Epitopes</subject><subject>Glycoproteins</subject><subject>Hepacivirus - chemistry</subject><subject>Hepacivirus - immunology</subject><subject>Hepatitis</subject><subject>Hepatitis C</subject><subject>Hepatitis C - virology</subject><subject>Humans</subject><subject>Liver</subject><subject>Liver cancer</subject><subject>Liver cirrhosis</subject><subject>Neutralizing</subject><subject>Protein Multimerization</subject><subject>Torrents</subject><subject>Vaccine development</subject><subject>Vaccines</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - immunology</subject><subject>Viral Hepatitis Vaccines - chemistry</subject><subject>Viral Hepatitis Vaccines - immunology</subject><subject>Viruses</subject><issn>0036-8075</issn><issn>1095-9203</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctLAzEQxoMotlbP3mTBi5e1eWyyCQgipT5A8KCeQzbO2pTtZk2yov-9W6xFPQ3M_Oabx4fQMcHnhFAxjdZBa-HcVK2SsthBY4IVzxXFbBeNMWYil7jkI3QQ4xLjoabYPhoxQUUhsRyji8cUepv6AJmvs7SAbAGdSS65mM2ydxf6mM3JnGavzaf1XfAJXJtZv-oa-DhEe7VpIhxt4gQ9X8-fZrf5_cPN3ezqPrcFpSnn3JbUgjEgqKIFr6CsaEGVxaxiVEIlJFeYYY6JqisjpVSsErUoh1xpmGQTdPmt2_XVCl4stCmYRnfBrUz41N44_bfSuoV-9e-aYE5oKdmgcLZRCP6th5j0ykULTWNa8H3UtKSlKIr1yAk6_YcufR_a4b41JdTwT8wHavpN2eBjDFBvtyFYr63RG2v0xpqh4-T3EVv-xwv2BdI0iz8</recordid><startdate>20221021</startdate><enddate>20221021</enddate><creator>Torrents de la Peña, Alba</creator><creator>Sliepen, Kwinten</creator><creator>Eshun-Wilson, Lisa</creator><creator>Newby, Maddy L</creator><creator>Allen, Joel D</creator><creator>Zon, Ian</creator><creator>Koekkoek, Sylvie</creator><creator>Chumbe, Ana</creator><creator>Crispin, Max</creator><creator>Schinkel, Janke</creator><creator>Lander, Gabriel C</creator><creator>Sanders, Rogier W</creator><creator>Ward, Andrew B</creator><general>The American Association for the Advancement of Science</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-6988-1457</orcidid><orcidid>https://orcid.org/0000-0002-1072-2694</orcidid><orcidid>https://orcid.org/0000-0003-0624-245X</orcidid><orcidid>https://orcid.org/0000-0003-2547-968X</orcidid><orcidid>https://orcid.org/0000-0001-5598-1780</orcidid><orcidid>https://orcid.org/0000-0003-0870-5075</orcidid><orcidid>https://orcid.org/0000-0002-2324-8573</orcidid><orcidid>https://orcid.org/0000-0001-7153-3769</orcidid><orcidid>https://orcid.org/0000-0003-4346-0739</orcidid><orcidid>https://orcid.org/0000-0003-4921-1135</orcidid><orcidid>https://orcid.org/0000-0003-1414-0648</orcidid></search><sort><creationdate>20221021</creationdate><title>Structure of the hepatitis C virus E1E2 glycoprotein complex</title><author>Torrents de la Peña, Alba ; Sliepen, Kwinten ; Eshun-Wilson, Lisa ; Newby, Maddy L ; Allen, Joel D ; Zon, Ian ; Koekkoek, Sylvie ; Chumbe, Ana ; Crispin, Max ; Schinkel, Janke ; Lander, Gabriel C ; Sanders, Rogier W ; Ward, Andrew B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-55c72ceaae629245be7b2429c03b328eb68590305019fba88893b6f670307a383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Antibodies</topic><topic>Antiviral Agents - 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| ispartof | Science (American Association for the Advancement of Science), 2022-10, Vol.378 (6617), p.263-269 |
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| source | MEDLINE; Science Magazine |
| subjects | Antibodies Antiviral Agents - chemistry Broadly Neutralizing Antibodies Cancer vaccines Chronic infection Cirrhosis Cryoelectron Microscopy Drug development Electron microscopy Epitopes Glycoproteins Hepacivirus - chemistry Hepacivirus - immunology Hepatitis Hepatitis C Hepatitis C - virology Humans Liver Liver cancer Liver cirrhosis Neutralizing Protein Multimerization Torrents Vaccine development Vaccines Viral Envelope Proteins - chemistry Viral Envelope Proteins - immunology Viral Hepatitis Vaccines - chemistry Viral Hepatitis Vaccines - immunology Viruses |
| title | Structure of the hepatitis C virus E1E2 glycoprotein complex |
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