Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Barnes, Christopher O.; Gristick, Harry B.; Freund, Natalia T.; Escolano, Amelia; Lyubimov, Artem Y.; Hartweger, Harald; West, Anthony P.; Cohen, Aina E.; Nussenzweig, Michel C.; Bjorkman, Pamela J.

doi:10.1038/s41467-018-03632-y

Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Journal Article · Wed Mar 28 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-03632-y· OSTI ID:1624084

Barnes, Christopher O. ^[1]; Gristick, Harry B. ^[2]; Freund, Natalia T. ^[3]; Escolano, Amelia ^[4]; Lyubimov, Artem Y. ^[5]; Hartweger, Harald ^[6]; West, Anthony P. ^[2]; Cohen, Aina E. ^[5]; Nussenzweig, Michel C. ^[7]; Bjorkman, Pamela J. ^[2]

California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering; DOE/OSTI
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology; Tel Aviv Univ., Ramat Aviv (Israel). Sackler Faculty of Medicine, Dept. of Clinical Immunology and Microbiology
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology
Rockefeller Univ., New York, NY (United States). Laboratory of Molecular Immunology; Rockefeller Univ., New York, NY (United States). Howard Hughes Medical Institute

Broadly neutralizing antibodies (bNAbs) isolated from HIV-1-infected individuals inform HIV-1 vaccine design efforts. Developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env). Here we present crystal structures, including a 3.8-Å X-ray free electron laser dataset, of natively glycosylated Env trimers complexed with BG18, the most potent V3/N332_gp120 glycan-targeting bNAb reported to date. Our structures show conserved contacts mediated by common D gene-encoded residues with the N332_gp120 glycan and the gp120 GDIR peptide motif, but a distinct Env-binding orientation relative to PGT121/10-1074 bNAbs. BG18’s binding orientation provides additional contacts with N392_gp120 and N386_gp120 glycans near the V3-loop base and engages protein components of the V1-loop. The BG18-natively-glycosylated Env structures facilitate understanding of bNAb–glycan interactions critical for using V3/N332_gp120 bNAbs therapeutically and targeting their epitope for immunogen design.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL) and Linac Coherent Light Source (LCLS)

Sponsoring Organization:: Bill and Melinda Gates Foundation; Burroughs Wellcome Fund; Gordon and Betty Moore Foundation; National Institute of Allergy and Infectious Diseases (NIAID); National Institute of General Medical Sciences (NIGMS); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1624084

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 9; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses Steichen, Jon M.; Lin, Ying-Cing; Havenar-Daughton, Colin Science, Vol. 366, Issue 6470 https://doi.org/10.1126/science.aax4380	journal	October 2019
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Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

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