Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies
Abstract
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.
- Authors:
-
- 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
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- 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
- OSTI Identifier:
- 1547413
- Grant/Contract Number:
- 681137; Al131873; 109718-63-RKNT; 109514-61-RKVA; AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Cell Host & Microbe
- Additional Journal Information:
- Journal Volume: 25; Journal Issue: 6; Journal ID: ISSN 1931-3128
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; HIV envelope glycoprotein; broadly neutralizing antibody; X-ray crystallography; cryoelectron microscopy; fusion peptide; ACS202; AMC011; VRC34.01
Citation Formats
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., and Wilson, Ian A. Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies. United States: N. p., 2019.
Web. doi:10.1016/j.chom.2019.04.011.
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. Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies. United States. https://doi.org/10.1016/j.chom.2019.04.011
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., and Wilson, Ian A. Wed .
"Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies". United States. https://doi.org/10.1016/j.chom.2019.04.011. https://www.osti.gov/servlets/purl/1547413.
@article{osti_1547413,
title = {Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies},
author = {Yuan, Meng and Cottrell, Christopher A. and Ozorowski, Gabriel and van Gils, Marit J. and Kumar, Sonu and Wu, Nicholas C. and Sarkar, Anita and Torres, Jonathan L. and de Val, Natalia and Copps, Jeffrey and Moore, John P. and Sanders, Rogier W. and Ward, Andrew B. and Wilson, Ian A.},
abstractNote = {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.},
doi = {10.1016/j.chom.2019.04.011},
journal = {Cell Host & Microbe},
number = 6,
volume = 25,
place = {United States},
year = {Wed Jun 12 00:00:00 EDT 2019},
month = {Wed Jun 12 00:00:00 EDT 2019}
}
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