Sequence and structural analysis of OmpW protein of Pasteurella multocida strains reveal evolutionary conservation among members of Pasteurellaceae along with its homologues

Abstract

Several bacterial outer membrane proteins (OMPs) are known to play diverse role in physiology including adoptive response to adverse environmental conditions and contribute for enhanced virulence. Pasteurella multocida, a causative agent of multiple infections in animals and avians, is also known to possess several uncharacterized OMPs as virulent factors. In the present study, hitherto uncharacterized OmpW gene encoding for OmpW protein of P. multocidastrains (n = 7) have been cloned, sequenced and comparatively analyzed with existing OmpW sequences/homologues (n = 98) by multiple bioinformatics tools. A comparative phylogenetic, multiple sequence alignment and structural features of OmpW protein of P. multocida with that of homologues in other bacterial species revealed the presence of evolutionarily conserved residues forming a pore like structure in outer membrane. Structurally, OmpW protein of P. multocidahad eight strands (β1-β8) with four external loops (L1–L4). Analysis of transmembrane pore (hydrophobic) features as well as predicted functionality by docking studies using fumerate molecule indicated similarity with that of OmpW protein of E. coli. Further, the study indicated the potential possibilities to target OmpW gene/protein of P. multocida either for development of alternative specific diagnostics or vaccines against pasteurellosis in livestock.