Journal
CELL REPORTS
Volume 21, Issue 1, Pages 222-235Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2017.09.024
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Funding
- International AIDS Vaccine Initiative (IAVI) through the Neutralizing Antibody Consortium (NAC) [IAVI SFP 2120/2121]
- National Institute of Allergy and Infectious Diseases (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery grant) [UM1AI100663]
- Ragon Institute of MGH
- MIT
- Harvard (MGH/RAGON SFP)
- USAID (PATH/USAID SFP)
- FP7 Marie Curie International Outgoing Fellowship for Career Development [623038]
- Bill and Melinda Gates Foundation Collaboration for AIDS Vaccine Discovery (CAVD) [OPP1084519]
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Recent efforts toward HIV vaccine development include the design of immunogens that can engage B cell receptors with the potential to affinity mature into broadly neutralizing antibodies (bnAbs). V2-apex bnAbs, which bind a protein-glycan region on HIV envelope glycoprotein (Env) trimer, are among the most broad and potent described. We show here that a rare glycan hole at the V2 apex is enriched in HIV isolates neutralized by inferred precursors of prototype V2-apex bnAbs. To investigate whether this feature could focus neutralizing responses onto the apex bnAb region, we immunized wild-type rabbits with soluble trimers adapted from these Envs. Potent autologous tier 2 neutralizing responses targeting basic residues in strand C of the V2 region, which forms the core epitope for V2-apex bnAbs, were observed. Neutralizing monoclonal antibodies (mAbs) derived from these animals display features promising for subsequent broadening of the response.
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