Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies

Yuan, Meng; Cottrell, Christopher A.; Ozorowski, Gabriel; van Gils, Marit J.; Kumar, Sonu; Wu, Nicholas C.; Sarkar, Anita; Torres, Jonathan L.; de Val, Natalia; Copps, Jeffrey; Moore, John P.; Sanders, Rogier W.; Ward, Andrew B.; Wilson, Ian A.

doi:10.1016/j.chom.2019.04.011

Title: Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies

Journal Article · Wed Jun 12 00:00:00 EDT 2019 · Cell Host & Microbe

DOI:https://doi.org/10.1016/j.chom.2019.04.011· OSTI ID:1547413

Yuan, Meng ^[1]; Cottrell, Christopher A. ^[1]; Ozorowski, Gabriel ^[1]; van Gils, Marit J. ^[2]; Kumar, Sonu ^[1]; Wu, Nicholas C. ^[1]; Sarkar, Anita ^[1]; Torres, Jonathan L. ^[1]; de Val, Natalia ^[1]; Copps, Jeffrey ^[1]; Moore, John P. ^[3]; Sanders, Rogier W. ^[4]; Ward, Andrew B. ^[1]; Wilson, Ian A. ^[1]

The Scripps Research Inst., La Jolla, CA (United States)
Univ. of Amsterdam (Netherlands)
Cornell Univ., Ithaca, NY (United States). Weill Medical College
Univ. of Amsterdam (Netherlands); Cornell Univ., Ithaca, NY (United States). Weill Medical College

The fusion peptide (FP) of HIV-1 envelope glycoprotein (Env) is essential for mediating viral entry. Detection of broadly neutralizing antibodies (bnAbs) that interact with the FP has revealed it as a site of vulnerability. We delineate X-ray and cryo-electron microscopy (cryo-EM) structures of bnAb ACS202, from an HIV-infected elite neutralizer, with an FP and with a soluble Env trimer (AMC011 SOSIP.v4.2) derived from the same patient. We show that ACS202 CDRH3 forms a “β strand” interaction with the exposed hydrophobic FP and recognizes a continuous region of gp120, including a conserved N-linked glycan at N88. A cryo-EM structure of another previously identified bnAb VRC34.01 with AMC011 SOSIP.v4.2 shows that it also penetrates through glycans to target the FP. We further demonstrate that the FP can twist and present different conformations for recognition by bnAbs, which enables approach to Env from diverse angles. The variable recognition of FP by bnAbs thus provides insights for vaccine design.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: HIV Vaccine Research and Design (HIVRAD) Program; International AIDS Vaccine Initiative Neutralizing Antibody Center; Bill and Melinda Gates Foundation; European Union’s Horizon 2020; National Institutes of Health (NIH); Achievement Rewards for College Scientists Foundation; Netherlands Organization for Scientific Research (NWO); amfAR Mathilde Krim Fellowships in Basic Biomedical Research; National Cancer Institute (NCI); National Institute of General Medical Sciences (NIGMS); USDOE Office of Science (SC); Center for Infectious Disease Control of the Netherlands National Institute for Public Health and the Environment

Grant/Contract Number:: 681137; Al131873; 109718-63-RKNT; 109514-61-RKVA; AC02-06CH11357

OSTI ID:: 1547413

Journal Information:: Cell Host & Microbe, Vol. 25, Issue 6; ISSN 1931-3128

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 24 works

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59 BASIC BIOLOGICAL SCIENCES
HIV envelope glycoprotein
broadly neutralizing antibody
X-ray crystallography
cryoelectron microscopy
fusion peptide
ACS202
AMC011
VRC34.01

Title: Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies

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