期刊
SCIENCE
卷 334, 期 6059, 页码 1097-1103出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1213256
关键词
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资金
- International AIDS Vaccine Initiative Neutralizing Antibody Center
- NIH [AI84817, AI74372]
- National Institute of Allergy and Infectious Diseases [AI33292]
- Canadian Institutes of Health Research [FRN HFE-224662]
- HIV Vaccine Research and Design grant [AI082362]
- UK Research Councils' Basic Technology Initiative [GRS/79268]
- Engineering and Physical Sciences Research Council [EP/G037604/1]
- National Cancer Institute (NCI) [U01 CA128416, Y1-CO-1020]
- Ragon Institute
- NIH through the National Center for Research Resources' [RR017573]
- DOE Office of Biological and Environmental Research
- NIH's National Center for Research Resources [P41RR001209]
- National Institute of General Medical Sciences (NIGMS) [Y1-GM-1104]
- DOE, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- Engineering and Physical Sciences Research Council [EP/G037604/1, GR/S79268/02] Funding Source: researchfish
- EPSRC [EP/G037604/1] Funding Source: UKRI
The HIV envelope (Env) protein gp120 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly neutralizing antibodies appear to interact directly with the HIV glycan coat. Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Man(9) at 1.65 and 1.29 angstrom resolution, respectively, and glycan binding data delineate a specific high mannose-binding site. Fab PGT 128 complexed with a fully glycosylated gp120 outer domain at 3.25 angstroms reveals that the antibody penetrates the glycan shield and recognizes two conserved glycans as well as a short beta-strand segment of the gp120 V3 loop, accounting for its high binding affinity and broad specificify. Furthermore, our data suggest that the high neutralization potency of PGT 127 and 128 immunoglobulin Gs may be mediated by cross-linking Env trimers on the viral surface.
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