Sialic acid recognition of the pandemic influenza 2009 H1N1 virus: Binding mechanism between human receptor and influenza hemagglutinin

Kaori Fukuzawa, Katsumi Omagari, Katsuhisa Nakajima, Eri Nobusawa, Shigenori Tanaka

研究成果: Article査読

14 被引用数 (Scopus)

抄録

Quantum mechanical fragment molecular orbital calculations have been performed for receptor binding of the hemagglutinin protein of the recently pandemic influenza 2009 H1N1 (2009/HIN1pdm), A/swine/Iowa/1930, and A/Puerto Rico/8/1934 viruses to α2-6 linked sialyloligosaccharides, as analogs of human receptors. The strongest receptor binding affinity was observed for the 2009/H1N1pdm. The inter-fragment interaction energy analysis revealed that the amino acid mutation of 2009/H1N1pdm, Ser145Lys, was a major cause of such strong binding affinity. Strong ionic pair interaction between the sialic acid and Lys145 was observed only in the 2009/H1N1pdm, in addition to the hydrogen bond between the sialic acid and Gln226 observed in all the HAs. Therefore, pandemic 2009/H1N1pdm has been found to recognize the α2-6 receptor much stronger than the 1930-swine and 1934-human.

本文言語English
ページ(範囲)530-539
ページ数10
ジャーナルProtein and Peptide Letters
18
5
DOI
出版ステータスPublished - 2011 5月
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 生化学

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