Selective pressure to increase charge in immunodominant epitopes of the H3 hemagglutinin influenza protein.

ABSTRACT: The evolutionary speed and the consequent immune escape of H3N2 influenza A virus make it an interesting evolutionary system. Charged amino acid residues are often significant contributors to the free energy of binding for protein-protein interactions, including antibody-antigen binding and ligand-receptor binding. We used Markov chain theory and maximum likelihood estimation to model the evolution of the number of charged amino acids on the dominant epitope in the hemagglutinin protein of circulating H3N2 virus strains. The number of charged amino acids increased in the dominant epitope B of the H3N2 virus since introduction in humans in 1968. When epitope A became dominant in 1989, the number of charged amino acids increased in epitope A and decreased in epitope B. Interestingly, the num

SUBMITTER: Pan K 

PROVIDER: S-EPMC3033527 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature