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 (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.
Keywords: FMO; Generalized Born (GB); HF; IFIE; LSTc; NCBI Influenza virus; Pandemic influenza 2009 H1N1 virus (2009/H1N1pdm); RMSD; fragment molecular orbital (FMO) method; influenza hemagglutinin (HA); molecular mechanics (MM); quantum mechanical calculation; sialic acid recognition; sialo-sugar chain; sialyloligosaccharides
Document Type: Research Article
Publication date: May 1, 2011
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