Amino acids substitutions in the PB2 protein of H7N9 influenza A viruses are important for virulence in mammalian hosts

• Published in: Scientific reports Vol. 5; no. 1; p. 8039
• Main Authors: Yamayoshi, Seiya, Fukuyama, Satoshi, Yamada, Shinya, Zhao, Dongming, Murakami, Shin, Uraki, Ryuta, Watanabe, Tokiko, Tomita, Yuriko, Neumann, Gabriele, Kawaoka, Yoshihiro
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 27.01.2015; Nature Publishing Group
• Subjects: 631/326/596; 631/326/596/1578; Adaptation; Amino Acid Substitution; Amino acids; Animals; Asparagine; Aspartic acid; Avian cells; Body Weight; Cell Line; Dogs; Female; Genes, Reporter; Glutamic acid; Growth kinetics; Humanities and Social Sciences; Humans; Infections; Influenza; Influenza A; Influenza A Virus, H7N9 Subtype - metabolism; Influenza A Virus, H7N9 Subtype - pathogenicity; Lung - virology; Lysine; Madin Darby Canine Kidney Cells; Mammals; Mice; Mice, Inbred BALB C; multidisciplinary; Mutation; Nasal Cavity - virology; Pathogenicity; Pathogens; Plasmids; Proteins; Science; Viral Proteins - genetics; Virology; Virulence; Virulence - genetics; Virus Replication; Viruses
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep08039

We tested the biological significance of two amino acid mutations in the PB2 protein (glutamic acid to lysine at position 627 and aspartic acid to asparagine at position 701) of A(H7N9) viruses for mammalian adaptation. Mutants were assessed for their viral polymerase activities, growth kinetics in mammalian and avian cells and pathogenicity in mice. We found that lysine at position 627 and asparagine at position 701 in PB2 are essential for mammalian adaptation of A(H7N9) viruses.