Large-scale analysis of influenza A virus sequences reveals potential drug target sites of non-structural proteins

• DOI: 10.1099/vir.0.011270-0
• Publication Date: 2009-08-12T19:43:27Z
• Authors: V. Darapaneni; V. K. Prabhaker; A. Kukol
• Keywords: Conserved sequence; Threading (protein sequence)

The non-structural protein 1 (NS1) of the influenza A virus and NS2 protein, which is also known as nuclear export play important roles in infectious life cycle virus. objective this study was to find degree conservation NS proteins identify conserved sites functional or structural importance that may be utilized potential drug target sites. analysis based on 2620 amino acid sequences for NS1 1195 protein. binding were mapped onto structures obtained from a combination experimentally available structure fragments with predicted threading models. In addition high regions function, novel highly have been identified, namely Glu159, Thr171, Val192, Arg200, Glu208 Gln218 Ser24, Leu28, Arg66, Arg84, Ser93, Ile97 Leu103 Using Q-SiteFinder site prediction algorithm, several found, including two spatially close could targeted bivalent ligand would interfere double-stranded RNA binding. Altogether, work reveals universally residues are candidates protein–protein interactions provide basis designing universal anti-influenza drugs.