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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)530-539
Number of pages10
JournalProtein and Peptide Letters
Volume18
Issue number5
DOIs
Publication statusPublished - 2011 May 1
Externally publishedYes

Keywords

  • Fragment molecular orbital (FMO) method
  • Influenza hemagglutinin (HA)
  • Pandemic influenza 2009 H1N1 virus (2009/H1N1pdm)
  • Quantum mechanical calculation
  • Sialic acid recognition
  • Sialo-sugar chain

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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