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

• Type of Material: Article
• Authors: Maino Tahara, National Institute of Infectious Diseases; Shinji Ohno, Kyushu University; Kouji Sakai, National Institute of Infectious Diseases; Yuri Ito, Hokkaido University; Hideo Fukuhara, Hokkaido University; Katsuhiro Komase, National Institute of Infectious Diseases; Melinda A. Brindley, Emory University; Paul Rota, Emory University; Richard Plemper, Emory University; Katsumi Maenaka, Hokkaido University; Makoto Takeda, National Institute of Infectious Diseases
• Language: English
• Date: 2013-03-01
• Publisher: American Society for Microbiology
• Publication Version: Final Published Version
• Copyright Statement: © 2013, American Society for Microbiology. All Rights Reserved.
• Final Published Version (URL): http://dx.doi.org/10.1128/JVI.03029-12
• Title of Journal or Parent Work: Journal of Virology
• ISSN: 0022-538X
• Volume: 87
• Issue: 6
• Start Page: 3583
• End Page: 3586
• Keywords: VIROLOGY; Virology; SLAM; BLIND; Life Sciences & Biomedicine; B-CELL RESPONSE; DOMAINS; NECTIN-4; FUSION; Science & Technology; ANTIBODIES; ERADICATION; LOCALIZATION; EPITHELIAL RECEPTOR
• Research Categories: Health Sciences, Immunology; Biology, Virology

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.