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 journalArticlepeer-review

13 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
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

Fingerprint Dive into the research topics of 'Sialic acid recognition of the pandemic influenza 2009 H1N1 virus: Binding mechanism between human receptor and influenza hemagglutinin'. Together they form a unique fingerprint.

Cite this