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-Structure paper
Title | Structure of the hepatitis C virus E1E2 glycoprotein complex. |
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Journal, issue, pages | Science, Vol. 378, Issue 6617, Page 263-269, Year 2022 |
Publish date | Oct 21, 2022 |
Authors | Alba Torrents de la Peña / Kwinten Sliepen / Lisa Eshun-Wilson / Maddy L Newby / Joel D Allen / Ian Zon / Sylvie Koekkoek / Ana Chumbe / Max Crispin / Janke Schinkel / Gabriel C Lander / Rogier W Sanders / Andrew B Ward / |
PubMed Abstract | 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 ...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. |
External links | Science / PubMed:36264808 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.83 - 20.0 Å |
Structure data | EMDB-25730, PDB-7t6x: EMDB-27578: nsEM map of E1E2 AMS0232 glycoprotein in complex with monoclonal antibody AR4A |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN/IMMUNE SYSTEM / hepatitis C virus / E1E2 / viral protein-immune system complex / antibody-antigen complex |