title: Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability.
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.
authors.affiliation: Department of Virology 3, National Institute of Infectious Diseases, Musashimurayama 208-0011, Tokyo, Japan. maino@nih.go.jp.
authors.forename: Maino
authors.initials: M
authors.lastname: Tahara
authors.affiliation: Department of Infection and Immunity, Luxembourg Institute of Health, Esch-sur-Alzette L-4354, Luxembourg. Jean-Philippe.Buerckert@lih.lu.
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Bürckert
authors.affiliation: Infectious Disease Surveillance Center, National Institute of Infectious Diseases, Shinjuku-ku 162-8640, Tokyo, Japan. kanou@nih.go.jp.
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Kanou
authors.affiliation: Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Hokkaido, Japan. maenaka@pharm.hokudai.ac.jp.
authors.forename: Katsumi
authors.initials: K
authors.lastname: Maenaka
authors.affiliation: Department of Infection and Immunity, Luxembourg Institute of Health, Esch-sur-Alzette L-4354, Luxembourg. Claude.Muller@lih.lu.
authors.forename: Claude P
authors.initials: CP
authors.lastname: Muller
authors.affiliation: Department of Virology 3, National Institute of Infectious Diseases, Musashimurayama 208-0011, Tokyo, Japan. mtakeda@nih.go.jp.
authors.forename: Makoto
authors.initials: M
authors.lastname: Takeda
mesh_terms: D057134:Antibodies, Neutralizing / Q000276:immunology*; D000914:Antibodies, Viral / Q000276:immunology*; D018985:Epitopes, B-Lymphocyte / Q000276:immunology*; D006389:Hemagglutinins, Viral / Q000276:immunology*; D006801:Humans; D008459:Measles virus / Q000276:immunology*
chemical_list: D057134:Antibodies, Neutralizing; D000914:Antibodies, Viral; D018985:Epitopes, B-Lymphocyte; C104413:H protein, Dolphin morbillivirus; D006389:Hemagglutinins, Viral
keywords: epitope; hemagglutinin protein; measles virus