Hepatitis C Virus E2 Envelope Glycoprotein Core Structure

Author:

Kong Leopold123,Giang Erick4,Nieusma Travis1,Kadam Rameshwar U.1,Cogburn Kristin E.14,Hua Yuanzi1,Dai Xiaoping1,Stanfield Robyn L.123,Burton Dennis R.234,Ward Andrew B.123,Wilson Ian A.1235,Law Mansun4

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

2. International AIDS Vaccine Initiative Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

3. Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.

5. Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

Deciphering Hepatitis C Hepatitis C virus is a major cause of liver disease and cancer. Two envelope glycoproteins, E1 and E2, form a heterodimer that facilitates infection. The envelope proteins have been difficult to crystallize, hindering vaccine development. Kong et al. (p. 1090 ) designed an E2 core glycoprotein construct and solved the crystal structure of the glycosylated protein in complex with a broadly neutralizing antibody. The host cell receptor binding site was identified by electron microscopy and mutagenesis. The findings should help in future drug and vaccine design.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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