Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, avian H5N1, and swine H1N2

Wei Hu

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DOI: 10.4236/jbise.2010.32017                

Abstract

The hemagglutinin (HA) of influenza viruses facilitates receptor binding and membrane fusion, which is the initial step of virus infection. Human influenza viruses preferentially bind to receptors with α2-6 lin- kages to galactose (SAα2,6Gal), whereas avian influenza viruses prefer receptors with α2-3 linkages to galactose (SAα2,3Gal). The current 2009 H1N1 pandemic is caused by a novel influenza A virus that has its genetic materials from birds, humans, and pigs. Its pandemic nature is characterized clearly by its dual binding to the α2-3 as well as α2-6 receptors, because the seasonal human H1N1 virus only binds to the α2-6 receptor. In a previous study, the informational spectrum method (ISM), a bioinformatics technique, was applied to uncover one highly conserved region in the HA protein associated with receptor binding preference in each of various influenza subtypes. In the present study, we extended the previous work by discovering multiple such domains in HA of 2009 H1N1 and avian H5N1 to expand our repertoire of known key regions in HA responsible for receptor binding affinity. Three such domains in HA of 2009 H1N1 were found at residue positions 106 to 130, 150 to 174, and 191 to 221, and another three domains in HA of avian H5N1 were located at residue positions 46 to 65, 136 to 153, and 269 to 286. These identified domains could be utilized as therapeutic and diagnostic targets for the prevention and treatment of influenza infection.

Keywords

Binding Specificity; Discrete Fourier Transform; Electron-Ion Interaction Potential; Entropy; Hemagglutinin; Influenza; Informational Spectrum Method

Conflicts of Interest

The authors declare no conflicts of interest.

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