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

Christopher O. Barnes, Harry B. Gristick, Natalia T. Freund, Amelia Escolano, Artem Y. Lyubimov, Harald Hartweger, Anthony P. West, Aina E. Cohen, Michel C. Nussenzweig and Pamela J. Bjorkman ()
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Christopher O. Barnes: California Institute of Technology
Harry B. Gristick: California Institute of Technology
Natalia T. Freund: The Rockefeller University
Amelia Escolano: The Rockefeller University
Artem Y. Lyubimov: Stanford Synchrotron Radiation Lightsource
Harald Hartweger: The Rockefeller University
Anthony P. West: California Institute of Technology
Aina E. Cohen: Stanford Synchrotron Radiation Lightsource
Michel C. Nussenzweig: The Rockefeller University
Pamela J. Bjorkman: California Institute of Technology

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract 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/N332gp120 glycan-targeting bNAb reported to date. Our structures show conserved contacts mediated by common D gene-encoded residues with the N332gp120 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 N392gp120 and N386gp120 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/N332gp120 bNAbs therapeutically and targeting their epitope for immunogen design.

Date: 2018
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DOI: 10.1038/s41467-018-03632-y

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