Mimicry of an HIV broadly neutralizing antibody epitope with a synthetic glycopeptide.
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.
Duke Scholars
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Related Subject Headings
- Protein Multimerization
- Protein Domains
- Molecular Mimicry
- Macaca mulatta
- HIV-1
- HIV Envelope Protein gp120
- HIV Antigens
- Glycopeptides
- Epitopes
- Clone Cells
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Location
Related Subject Headings
- Protein Multimerization
- Protein Domains
- Molecular Mimicry
- Macaca mulatta
- HIV-1
- HIV Envelope Protein gp120
- HIV Antigens
- Glycopeptides
- Epitopes
- Clone Cells