期刊
STRUCTURE
卷 25, 期 11, 页码 1719-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.09.009
关键词
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资金
- NIH [NIAID R01 AI116274, R01AI129769, NIGMS R01 GM117836, NIAID P01 AI120756]
- Bill and Melinda Gates Foundation [OPP1033109]
- CIHR foundation [352417]
- Canada Research Chairs program
- Saudi Government
- FRQS
- US Department of Energy Office of Biological and Environmental Research
- NIH National Center for Research Resources, Biomedical Technology [P41RR001209]
- National Institute of General Medical Sciences
Antibodies can have an impact on HIV-1 infection in multiple ways, including antibody-dependent cellular cytotoxicity (ADCC), a correlate of protection observed in the RV144 vaccine trial. One of the most potent ADCC-inducing epitopes on HIV-1 Env is recognized by the C11 antibody. Here, we present the crystal structure, at 2.9 angstrom resolution, of the C11-like antibody N12-i3, in a quaternary complex with the HIV-1 gp120, a CD4-mimicking peptide M48U1, and an A32-like antibody, N5-i5. Antibody N12-i3 recognizes an epitope centered on the N-terminal eighth strand'' of a critical beta sandwich, which our analysis indicates to be emblematic of a late-entry state, after the gp120 detachment. In prior entry states, this sandwich comprises only seven strands, with the eighth strand instead pairing with a portion of the gp120 C terminus. The conformational gymnastics of HIV-1 gp120 thus includes altered beta-strand pairing, possibly to reduce immunogenicity, although nevertheless still recognized by the human immune system.
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