期刊
SCIENCE IMMUNOLOGY
卷 3, 期 21, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciimmunol.aar3534
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资金
- National Institute of Allergy and Infectious Diseases (NIAID) grant [R21AI130605]
- NIAID grant [5R44AI122360-02]
- U.S. Department of Energy (DOE) Office of Science User Facility [DE-AC02-05CH11231]
- University of California Office of the President [8.3.1]
- Multicampus Research Programs and Initiatives Grant [MR-15-328599]
- Program for Breakthrough Biomedical Research - Sandler Foundation
- DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
Respiratory syncytial virus (RSV) is a top cause of severe lower respiratory tract disease and mortality in young children and the elderly. The viral envelope G glycoprotein contributes to pathogenesis through its roles in host cell attachment and modulation of host immunity. Although the G glycoprotein is a target of protective RSV-neutralizing antibodies, its development as a vaccine antigen has been hindered by its heterogeneous glycosylation and sequence variability outside a conserved central domain (CCD). We describe the cocrystal structures of two high-affinity broadly neutralizing human monoclonal antibodies bound to the RSV G CCD. The antibodies bind to neighboring conformational epitopes, which we named antigenic sites gamma 1 and gamma 2, that span a highly conserved surface, illuminating an important region of vulnerability. We further show that isolated RSV G CCD activates the chemokine receptor CX3CR1 and that antibodies block this activity. These studies provide a template for rational vaccine design targeting this key contributor to RSV disease.
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