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

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Published inJournal of Virology Vol. 87; no. 6; pp. 3583 - 3586
Main Authors Tahara, Maino, Ohno, Shinji, Sakai, Kouji, Ito, Yuri, Fukuhara, Hideo, Komase, Katsuhiro, Brindley, Melinda A., Rota, Paul A., Plemper, Richard K., Maenaka, Katsumi, Takeda, Makoto
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.03.2013
Subjects
Antibodies, Neutralizing - immunology
Antibodies, Viral - immunology
Epitopes, B-Lymphocyte - immunology
Hemagglutinins, Viral - immunology
Measles virus
Measles virus - immunology
Virus-Cell Interactions
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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList 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.
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.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.
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Author Richard K. Plemper
Kouji Sakai
Makoto Takeda
Hideo Fukuhara
Melinda A. Brindley
Yuri Ito
Maino Tahara
Shinji Ohno
Paul A. Rota
Katsuhiro Komase
Katsumi Maenaka
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Here, we provide direct evidence that the receptor-binding site of measles virus (MV) hemagglutinin protein itself forms an effective conserved neutralizing...
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SubjectTerms Antibodies, Neutralizing - immunology
Antibodies, Viral - immunology
Epitopes, B-Lymphocyte - immunology
Hemagglutinins, Viral - immunology
Measles virus
Measles virus - immunology
Virus-Cell Interactions
Title The Receptor-Binding Site of the Measles Virus Hemagglutinin Protein Itself Constitutes a Conserved Neutralizing Epitope
URI http://jvi.asm.org/content/87/6/3583.abstract
https://www.ncbi.nlm.nih.gov/pubmed/23283964
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https://www.proquest.com/docview/1323816704
https://pubmed.ncbi.nlm.nih.gov/PMC3592127
Volume 87
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