Journal
IMMUNITY
Volume 45, Issue 1, Pages 31-45Publisher
CELL PRESS
DOI: 10.1016/j.immuni.2016.06.026
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Funding
- International AIDS Vaccine Initiative Neutralizing Antibody Consortium through Collaboration for AIDS Vaccine Discovery grant [OPP1084519]
- NIH [R01 AI033292]
- Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery Grant [UM1AI100663]
- California HIV/AIDS Research Program Basic Biomedical Sciences Training Award [D13-SRI-391]
- James and Jessie Minor Chair in Immunology
- IAVI
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The dense patch of high-mannose-type glycans surrounding the N332 glycan on the HIV envelope glycoprotein (Env) is targeted by multiple broadly neutralizing antibodies (bnAbs). This region is relatively conserved, implying functional importance, the origins of which are not well understood. Here we describe the isolation of new bnAbs targeting this region. Examination of these and previously described antibodies to Env revealed that four different bnAb families targeted the (324)GDIR(327) peptide stretch at the base of the gp120 V3 loop and its nearby glycans. We found that this peptide stretch constitutes part of the CCR5 co-receptor binding site, with the high-mannose patch glycans serving to camouflage it from most antibodies. GDIR-glycan bnAbs, in contrast, bound both (324)GDIR(327) peptide residues and high-mannose patch glycans, which enabled broad reactivity against diverse HIV isolates. Thus, as for the CD4 binding site, bnAb effectiveness relies on circumventing the defenses of a critical functional region on Env.
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