<i style="">In silico</i> 3-D structure prediction of H1N1 2009 neuraminidase and comparative analysis of coding statistics of mutated genes

Abstract

The enzyme neuraminidase (NA), coded by H1N1 virus, catalyses the removal of terminal sialic acid from viral and cellular glycoconjugates. It cleaves the terminal sialic acid on the glycosylated NA during virus budding to facilitate virus release. The outbreak of Swine flu is suspected to be caused due to H274Y mutation in the neuraminidase enzyme of H1N1 2009 strain. The present study involves 3-D structure modeling of mutated neuraminidase of the strain A/Poland/274/2009 (H1N1) by MODELLER9v7 and comparative analysis of coding statistics among NA gene of 3 mutated H1N1 strains with GenBank accession numbers GU112751, GU371269 and CY053923. The analysis of 3-D model revealed that NAs have a common fold characterised by β-pleated sheet flanked either side by helices. The amino terminal end of the molecule is occupied by β-α-β motif and carboxy terminal end by β-hairpin motif. The molecule is characterised by 24 strands and 3 helices. The α₁helix is the longest among the three helices. The comparative analysis of coding statistics indicates that the statistical features f₁, f₅, f₆ and f₇ have the most discriminating power for the individual recognition of the mutated neuraminidase genes of H1N1 2009.