Journal
SCIENCE TRANSLATIONAL MEDICINE
Volume 9, Issue 381, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/scitranslmed.aai7521
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Funding
- NIH, National Institute of Allergy and Infectious Diseases (NIAID) [UM-1 AI100645]
- Division of AIDS CHAVI-Immunogen Discovery grant [R01 AI120801-01]
- Medical Scientist Training Program training grant [T32GM007171]
- Ruth L. Kirschstein National Research Service Award [F30-AI122982-0]
- NIAID
- Vaccine Research Center, NIAID
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A goal for an HIV-1 vaccine is to overcome virus variability by inducing broadly neutralizing antibodies (bnAbs). One key target of bnAbs is the glycan-polypeptide at the base of the envelope (Env) third variable loop (V3). We have designed and synthesized a homogeneous minimal immunogen with high-mannose glycans reflective of a native Env V3-glycan bnAb epitope (Man9-V3). V3-glycan bnAbs bound to Man9-V3 glycopeptide and native-like gp140 trimers with similar affinities. Fluorophore-labeled Man9-V3 glycopeptides bound to bnAb memory B cells and were able to be used to isolate a V3-glycan bnAb from an HIV-1-infected individual. In rhesus macaques, immunization with Man9-V3 induced V3-glycan-targeted antibodies. Thus, the Man9-V3 glycopeptide closely mimics an HIV-1 V3-glycan bnAb epitope and can be used to isolate V3-glycan bnAbs.
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