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

Abstract:

:Quantum mechanical fragment molecular orbital calculations have been performed for receptor binding of the hemagglutinin protein of the recently pandemic influenza 2009 H1N1, 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.

journal_name

Protein Pept Lett

authors

Fukuzawa K,Omagari K,Nakajima K,Nobusawa E,Tanaka S

doi

10.2174/092986611794927893

subject

Has Abstract

pub_date

2011-05-01 00:00:00

pages

530-9

issue

5

eissn

0929-8665

issn

1875-5305

pii

BSP/ PPL/ E pub/0269

journal_volume

18

pub_type

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