Journal
CELL REPORTS
Volume 16, Issue 9, Pages 2327-2338Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2016.07.074
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Funding
- Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery Grant [UM1AI100663]
- NIH HIVRAD Grant [P01 AI110657]
- International AIDS Vaccine Initiative Neutralizing Antibody Consortium through Collaboration for AIDS Vaccine Discovery [OPP1084519, OPP1115782]
- Marie-Curie Fellowship (FP7-PEOPLE-IOF)
- Aids fonds Netherlands [2012041]
- EMBO [ASTF260-2013]
- Netherlands Organization for Scientific Research [917.11.314]
- European Research Council [ERC-StG-2011-280829-SHEV]
- IAVI
- USAID
- Bill AMP
- Melinda Gates Foundation
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A major advance in the search for an HIV vaccine has been the development of a near-native Envelope trimer (BG505 SOSIP. 664) that can induce robust autologous Tier 2 neutralization. Here, potently neutralizing monoclonal antibodies (nAbs) from rabbits immunized with BG505 SOSIP. 664 are shown to recognize an immunodominant region of gp120 centered on residue 241. Residue 241 occupies a hole in the glycan defenses of the BG505 isolate, with fewer than 3% of global isolates lacking a glycan site at this position. However, at least one conserved glycan site is missing in 89% of viruses, suggesting the presence of glycan holes in most HIV isolates. Serum evidence is consistent with targeting of holes in natural infection. The immunogenic nature of breaches in the glycan shield has been under-appreciated in previous attempts to understand autologous neutralizing antibody responses and has important potential consequences for HIV vaccine design.
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