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

• 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
• Journal Title: Journal of Virology
• Volume: Volume 87, Number 6
• Publisher: American Society for Microbiology | 2013-03-01, Pages 3583-3586
• Type of Work: Article | Final Publisher PDF
• Publisher DOI: http://doi.org/10.1128/JVI.03029-12
• Subjects: Biology, Virology; Health Sciences, Immunology
• Keywords: Science & Technology; Life Sciences & Biomedicine; Virology; VIROLOGY; B-CELL RESPONSE; EPITHELIAL RECEPTOR; SLAM; LOCALIZATION; ERADICATION; ANTIBODIES; NECTIN-4; DOMAINS; FUSION; BLIND

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.