Hemagglutinin is an important influenza virus antigen whose fast rate of evolution allows the virus to evade the human antibody response.
This phenomenon is called antigenic drift. Several key amino acid positions in hemagglutinin have been previously identified as evolving especially rapidly, presumably under pressure from the human immune system, but the identities of the selectively favored amino acids at those positions remained unknown. In this paper, we identify those specific amino acid substitutions at rapidly as well as slowly evolving sites that occurred in hemagglutinin unusually often over the past 40 years.
These amino acid substitutions are likely to have been adaptive. Our findings shed light on how the influenza A antigenic drift proceeds and may have implications for vaccine development.
Proceedings of the Royal Society B: Biological Sciences
Proceedings B is the Royal Society's flagship biological research journal, dedicated to the rapid publication and broad dissemination of high-quality research papers, reviews and comment and reply papers. The scope of journal is diverse and is especially strong in organismal biology.
publishing.royalsociety/proceedingsb
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