Home
Resources
Publications
Structural Characterization of a Highly-Potent V3-glycan Broadly Neutralizing Antibody Bound to Natively-Glycosylated HIV-1 Envelope

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 Jr, Aina E Cohen, Michel C Nussenzweig, Pamela J Bjorkman

Nat Commun. 2018 Mar 28;9(1):1251.

PMID: 29593217

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP145164245	A3 Glycan		145164-24-5	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: