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Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability
Globally eliminating measles using available vaccines is biologically feasible because the measles virus (MV) hemagglutinin (H) protein is antigenically stable. The H protein is responsible for receptor binding, and is the main target of neutralizing antibodies. The immunodominant epitope, known as...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4997578/ https://www.ncbi.nlm.nih.gov/pubmed/27490564 http://dx.doi.org/10.3390/v8080216 |
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author | Tahara, Maino Bürckert, Jean-Philippe Kanou, Kazuhiko Maenaka, Katsumi Muller, Claude P. Takeda, Makoto |
author_facet | Tahara, Maino Bürckert, Jean-Philippe Kanou, Kazuhiko Maenaka, Katsumi Muller, Claude P. Takeda, Makoto |
author_sort | Tahara, Maino |
collection | PubMed |
description | Globally eliminating measles using available vaccines is biologically feasible because the measles virus (MV) hemagglutinin (H) protein is antigenically stable. The H protein is responsible for receptor binding, and is the main target of neutralizing antibodies. The immunodominant epitope, known as the hemagglutinating and noose epitope, is located near the receptor-binding site (RBS). The RBS also contains an immunodominant epitope. Loss of receptor binding correlates with an escape from the neutralization by antibodies that target the epitope at RBS. Another neutralizing epitope is located near RBS and is shielded by an N-linked sugar in certain genotype strains. However, human sera from vaccinees and measles patients neutralized all MV strains with similar efficiencies, regardless of the N-linked sugar modification or mutations at these epitopes. Two other major epitopes exist at a distance from RBS. One has an unstructured flexible domain with a linear neutralizing epitope. When MV-H forms a tetramer (dimer of dimers), these epitopes may form the dimer-dimer interface, and one of the two epitopes may also interact with the F protein. The neutralization mechanisms of antibodies that recognize these epitopes may involve inhibiting the H-F interaction or blocking the fusion cascade after MV-H binds to its receptors. |
format | Online Article Text |
id | pubmed-4997578 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-49975782016-08-26 Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability Tahara, Maino Bürckert, Jean-Philippe Kanou, Kazuhiko Maenaka, Katsumi Muller, Claude P. Takeda, Makoto Viruses Review Globally eliminating measles using available vaccines is biologically feasible because the measles virus (MV) hemagglutinin (H) protein is antigenically stable. The H protein is responsible for receptor binding, and is the main target of neutralizing antibodies. The immunodominant epitope, known as the hemagglutinating and noose epitope, is located near the receptor-binding site (RBS). The RBS also contains an immunodominant epitope. Loss of receptor binding correlates with an escape from the neutralization by antibodies that target the epitope at RBS. Another neutralizing epitope is located near RBS and is shielded by an N-linked sugar in certain genotype strains. However, human sera from vaccinees and measles patients neutralized all MV strains with similar efficiencies, regardless of the N-linked sugar modification or mutations at these epitopes. Two other major epitopes exist at a distance from RBS. One has an unstructured flexible domain with a linear neutralizing epitope. When MV-H forms a tetramer (dimer of dimers), these epitopes may form the dimer-dimer interface, and one of the two epitopes may also interact with the F protein. The neutralization mechanisms of antibodies that recognize these epitopes may involve inhibiting the H-F interaction or blocking the fusion cascade after MV-H binds to its receptors. MDPI 2016-08-02 /pmc/articles/PMC4997578/ /pubmed/27490564 http://dx.doi.org/10.3390/v8080216 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Tahara, Maino Bürckert, Jean-Philippe Kanou, Kazuhiko Maenaka, Katsumi Muller, Claude P. Takeda, Makoto Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title | Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title_full | Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title_fullStr | Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title_full_unstemmed | Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title_short | Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability |
title_sort | measles virus hemagglutinin protein epitopes: the basis of antigenic stability |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4997578/ https://www.ncbi.nlm.nih.gov/pubmed/27490564 http://dx.doi.org/10.3390/v8080216 |
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