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Author Notes:

Address correspondence to Maino Tahara, maino@nih.go.jp

We thank T.A. Sato, Y. Yanagi, and T. Seya for providing MAbs, N. Ito and M. Sugiyama for providing BHK/T7-9 cells, and K. Taira for providing an MV isolate.

We also thank all the members of Department of Virology 3, NIID, Japan, for technical support.

Subjects:

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Virology
  • VIROLOGY
  • B-CELL RESPONSE
  • EPITHELIAL RECEPTOR
  • SLAM
  • LOCALIZATION
  • ERADICATION
  • ANTIBODIES
  • NECTIN-4
  • DOMAINS
  • FUSION
  • BLIND

The Receptor-Binding Site of the Measles Virus Hemagglutinin Protein Itself Constitutes a Conserved Neutralizing Epitope

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Journal Title:

Journal of Virology

Volume:

Volume 87, Number 6

Publisher:

, Pages 3583-3586

Type of Work:

Article | Final Publisher PDF

Abstract:

Here, we provide direct evidence that the receptor-binding site of measles virus (MV) hemagglutinin protein itself forms an effective conserved neutralizing epitope (CNE). Several receptor-interacting residues constitute the CNE. Thus, viral escape from neutralization has to be associated with loss of receptor-binding activity. Since interactions with both the signaling lymphocyte activation molecule (SLAM) and nectin4 are critical for MV pathogenesis, its escape, which results from loss of receptor-binding activity, should not occur in nature.

Copyright information:

© 2013, American Society for Microbiology. All Rights Reserved.

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