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Erratum published on 21 November 2016, see Viruses 2016, 8(11), 313.

Open AccessReview
Viruses 2016, 8(8), 216; doi:10.3390/v8080216

Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability

1
Department of Virology 3, National Institute of Infectious Diseases, Musashimurayama 208-0011, Tokyo, Japan
2
Department of Infection and Immunity, Luxembourg Institute of Health, Esch-sur-Alzette L-4354, Luxembourg
3
Infectious Disease Surveillance Center, National Institute of Infectious Diseases, Shinjuku-ku 162-8640, Tokyo, Japan
4
Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Hokkaido, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Richard K. Plemper
Received: 15 June 2016 / Revised: 19 July 2016 / Accepted: 20 July 2016 / Published: 2 August 2016
(This article belongs to the Special Issue Recent Progress in Measles Virus Research)
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Abstract

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. View Full-Text
Keywords: measles virus; hemagglutinin protein; epitope measles virus; hemagglutinin protein; epitope
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Tahara, M.; Bürckert, J.-P.; Kanou, K.; Maenaka, K.; Muller, C.P.; Takeda, M. Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability. Viruses 2016, 8, 216.

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