Functional and structural characterization of neutralizing epitopes of measles virus hemagglutinin protein.

ABSTRACT: Effective vaccination programs have dramatically reduced the number of measles-related deaths globally. Although all the available data suggest that measles eradication is biologically feasible, a structural and biochemical basis for the single serotype nature of measles virus (MV) remains to be provided. The hemagglutinin (H) protein, which binds to two discrete proteinaceous receptors, is the major neutralizing target. Monoclonal antibodies (MAbs) recognizing distinct epitopes on the H protein were characterized using recombinant MVs encoding the H gene from different MV genotypes. The effects of various mutations on neutralization by MAbs and virus fitness were also analyzed, identifying the location of five epitopes on the H protein structure. Our data in the present study demonstrated

SUBMITTER: Tahara M 

PROVIDER: S-EPMC3536376 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature