Dataset Information


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

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.


PROVIDER: S-EPMC5871869 | BioStudies | 2018-01-01

REPOSITORIES: biostudies

Similar Datasets

2016-01-01 | S-EPMC4990068 | BioStudies
2018-01-01 | S-EPMC5856820 | BioStudies
2017-01-01 | S-EPMC5562351 | BioStudies
2020-01-01 | S-EPMC7577740 | BioStudies
2017-01-01 | S-EPMC5562350 | BioStudies
2017-01-01 | S-EPMC5408352 | BioStudies
2019-01-01 | S-EPMC6597128 | BioStudies
2020-01-01 | S-EPMC7494343 | BioStudies
2020-01-01 | S-EPMC6960291 | BioStudies
2018-01-01 | S-EPMC5830440 | BioStudies