期刊
CELL
卷 165, 期 4, 页码 813-826出版社
CELL PRESS
DOI: 10.1016/j.cell.2016.04.010
关键词
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资金
- Intramural Research Program of the Vaccine Research Center
- National Institute of Allergy and Infectious Diseases
- National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health (NIH)
- International AIDS Vaccine Initiative's (IAVI's) Neutralizing Antibody Consortium
- Bill AMP
- Melinda Gates Foundation
- Ministry of Foreign Affairs of Denmark
- Irish Aid
- Ministry of Finance of Japan
- Ministry of Foreign Affairs of the Netherlands
- Norwegian Agency for Development Cooperation
- UK Department for International Development
- United States Agency for International Development (USAID)
- International AIDS Vaccine Initiative Neutralizing Antibody Center CAVD grant
- Scripps Center For HIV/AIDS Vaccine Immunology-Immunogen Discovery (CHAVI-ID) grant [1UM1AI100663]
- Duke CHAVI-ID grant [UM1 AI100645]
- Swiss National Foundation of Science Fellowship [148914]
- Academia Sinica
- Ministry of Science and Technology [MOST 104-0210-01-09-02, 103-2321-B-001-004]
- NIH [R01 AI072155]
- US Department of Energy, Basic Energy Sciences, Office of Science [W-31-109-Eng-38]
- [HHSN261200800001E]
The HIV-1-envelope (Env) trimer is covered by a glycan shield of similar to 90 N-linked oligosaccharides, which comprises roughly half its mass and is a key component of HIV evasion from humoral immunity. To understand how antibodies can overcome the barriers imposed by the glycan shield, we crystallized fully glycosylated Env trimers from clades A, B, and G, visualizing the shield at 3.4-3.7 angstrom resolution. These structures reveal the HIV-1-glycan shield to comprise a network of interlocking oligosaccharides, substantially ordered by glycan crowding, that encase the protein component of Env and enable HIV-1 to avoid most antibody-mediated neutralization. The revealed features delineate a taxonomy of N-linked glycan-glycan interactions. Crowded and dispersed glycans are differently ordered, conserved, processed, and recognized by antibody. The structures, along with glycan-array binding and molecular dynamics, reveal a diversity in oligosaccharide affinity and a requirement for accommodating glycans among known broadly neutralizing antibodies that target the glycan-shielded trimer.
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