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Structures of respiratory syncytial virus G antigen bound to broadly neutralizing antibodies.

  • Author(s): Fedechkin, Stanislav O
  • George, Natasha L
  • Wolff, Jacob T
  • Kauvar, Lawrence M
  • DuBois, Rebecca M
  • et al.

Published Web Location

https://www.ncbi.nlm.nih.gov/pubmed/?term=29523582
No data is associated with this publication.
Abstract

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 γ1 and γ2, 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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