Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 50, Pages 20248-20253Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1320524110
Keywords
insertional mutagenesis; protein flexibility; viral evolution
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Funding
- Center for Research on Influenza Pathogenesis Grant [HHSN266200700010C]
- National Institutes for Health [1P01AI097092-01A1]
- Program for Appropriate Technology in Health (PATH)
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The molecular basis for the diversity across influenza strains is poorly understood. To gain insight into this question, we mutagenized the viral genome and sequenced recoverable viruses. Only two small regions in the genome were enriched for insertions, the hemagglutinin head and the immune-modulatory nonstructural protein 1. These proteins play a major role in host adaptation, and thus need to be able to evolve rapidly. We propose a model in which certain influenza A virus proteins (or protein domains) exist as highly plastic scaffolds, which will readily accept mutations yet retain their functionality. This model implies that the ability to rapidly acquire mutations is an inherent aspect of influenza HA and nonstructural protein 1 proteins; further, this may explain why rapid antigenic drift and a broad host range is observed with influenza A virus and not with some other RNA viruses.
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