Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 100, Issue 12, Pages 7152-7157Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1132114100
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- NIGMS NIH HHS [1-R01-GM60729-01] Funding Source: Medline
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Although the surface proteins of human influenza A virus evolve rapidly and continually produce antigenic variants, the internal viral genes acquire mutations very gradually. In this paper, we analyze the sequence evolution of three influenza A genes over the past two decades. We study codon usage as a discriminating signature of gene and even residue-specific diversifying and purifying selection. Non-random codon choice can increase or decrease the effective local substitution rate. We demonstrate that the codons of hemagglutinin, particularly those in the antibody-combining regions, are significantly biased toward substitutional point mutations relative to the codons of other influenza virus genes. We discuss the evolutionary interpretation and implications of these biases for hemagglutinin's antigenic evolution. We also introduce information-theoretic methods that use sequence data. to detect regions of recent positive selection and potential protein conformational changes.
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