期刊
NATURE COMMUNICATIONS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms8479
关键词
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资金
- Department of Biochemistry, University of Oxford
- International AIDS Vaccine Initiative Neutralizing Antibody Center
- NAC CAVD grant
- National Institute of Allergy and Infectious Diseases (CHAVI-ID) [P01AI081625, 1UM1AI100663]
- Medical Research Council [MR/K024426/1, MR/L009528/1]
- Wellcome Trust Centre [090532/Z/09/Z]
- MRC [MR/K024426/1, MR/L009528/1] Funding Source: UKRI
- Medical Research Council [MR/L009528/1, MR/K024426/1] Funding Source: researchfish
The envelope spike of HIV-1 employs a 'glycan shield' to protect itself from antibodymediated neutralization. Paradoxically, however, potent broadly neutralizing antibodies (bnAbs) that target this shield have been isolated. The unusually high glycan density on the gp120 subunit limits processing during biosynthesis, leaving a region of under-processed oligomannose-type structures, which is a primary target of these bnAbs. Here we investigate the contribution of individual glycosylation sites in the formation of this so-called intrinsic mannose patch. Deletion of individual sites has a limited effect on the overall size of the intrinsic mannose patch but leads to changes in the processing of neighbouring glycans. These structural changes are largely tolerated by a panel of glycan-dependent bnAbs targeting these regions, indicating a degree of plasticity in their recognition. These results support the intrinsic mannose patch as a stable target for vaccine design.
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