Complex-type N -glycan recognition by potent broadly neutralizing HIV antibodies
Rockefeller University · California Institute of Technology · +6 more institutions
Abstract
Broadly neutralizing HIV antibodies (bNAbs) can recognize carbohydrate-dependent epitopes on gp120. In contrast to previously characterized glycan-dependent bNAbs that recognize high-mannose N-glycans, PGT121 binds complex-type N-glycans in glycan microarrays. We isolated the B-cell clone encoding PGT121, which segregates into PGT121-like and 10-1074-like groups distinguished by sequence, binding affinity, carbohydrate recognition, and neutralizing activity. Group 10-1074 exhibits remarkable potency and breadth but no detectable binding to protein-free glycans. Crystal structures of unliganded PGT121, 10-1074, and their likely germ-line precursor reveal that differential carbohydrate recognition maps to a…
Citation impact
- FWCI
- 13.88
- Percentile
- 100%
- References
- 79
Authors
14Topics & keywords
- Glycan
- Epitope
- Neutralization
- Antibody
- Glycoprotein
- Mannose
- Biology
- Glycobiology
- Good health and well-being
Funding
- UDU.S. Department of Energy
- BABill and Melinda Gates FoundationAwards: 38660, 1032144
- GAGordon and Betty Moore Foundation
- CICalifornia Institute of Technology
- WTWellcome TrustAward: WT093378MA
- NINational Institutes of HealthAward: U01 CA128416
- EAEngineering and Physical Sciences Research CouncilAwards: EP/G037604/1, EP/G037604/1
- NCNational Cancer Institute