期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-07962-9
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资金
- Spanish MINECO [BIO2015-64421-R]
- Basque Government [IT838-13]
- MRC [MC_UU_12010, G0902418, MC_UU_12025]
- Wellcome Trust [104924/14/Z/14, 091911]
- MRC/BBSRC/EPSRC [MR/K01577X/1]
- BBSRC (Deutsche Forschungsgemeinschaft (Research unit 1905 Structure and function of the peroxisomal translocon))
- Wolfson Foundation
- EPA Cephalosporin Fund
- John Fell Fund
- Canada Graduate Scholarship Master's Award
- Vanier Canada Graduate Scholarship from the Canadian Institutes of Health Research
- Canadian Institutes of Health Research [NIH-150414]
- Canada Research Chairs program
- Basque Government
- BBSRC [BB/P026354/1] Funding Source: UKRI
- MRC [MC_UU_00008/9, MC_PC_15065, MR/S005382/1] Funding Source: UKRI
Antibodies against the Membrane-Proximal External Region (MPER) of the Env gp41 subunit neutralize HIV-1 with exceptional breadth and potency. Due to the lack of knowledge on the MPER native structure and accessibility, different and exclusive models have been proposed for the molecular mechanism of MPER recognition by broadly neutralizing antibodies. Here, accessibility of antibodies to the native Env MPER on single virions has been addressed through STED microscopy. STED imaging of fluorescently labeled Fabs reveals a common pattern of native Env recognition for HIV-1 antibodies targeting MPER or the surface subunit gp120. In the case of anti-MPER antibodies, the process evolves with extra contribution of interactions with the viral lipid membrane to binding specificity. Our data provide biophysical insights into the recognition of the potent and broadly neutralizing MPER epitope on HIV virions, and as such is of importance for the design of therapeutic interventions.
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