期刊
JOURNAL OF VIROLOGY
卷 89, 期 13, 页码 6952-6959出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00230-15
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资金
- Department of Biochemistry, University of Oxford
- International AIDS Vaccine Initiative Neutralizing Antibody Center
- NAC CAVD grant
- CHAVI-ID grant [1UM1AI100663]
- Medical Research Council [MR/K024426/1]
- Medical Research Council [MR/K024426/1] Funding Source: researchfish
- MRC [MR/K024426/1] Funding Source: UKRI
Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.
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