作者: Kiattawee Choowongkomon , Pongrama Ramasoota , Chalermpol Lekcharoensuk , Nantawan Petcharat , Porntippa Leckcharoensuk
DOI:
关键词: Infectivity 、 Influenza A virus 、 Virtual screening 、 Electrophoretic mobility shift assay 、 Binding domain 、 In vitro 、 Biology 、 Biochemistry 、 RNA silencing 、 RNA
摘要: Nonstructural protein 1 (NS1) of the highly pathogenic avian influenza virus (H5N1) contains a conserved RNA binding domain (RBD) that inhibits antiviral functions host-innate immune response. Dimerization NS1 forms central groove and binds to double stranded (ds) RNA. This region might serve as potential drug target. In this study, three dimensional structure model RBD was constructed virtual screening performed identify lead compounds bound within around groove. The showed 5 with energy ranging between -16.05 -17.36 Kcal/mol. Two commercially available compounds, estradiol veratridine, were selected for using in an vitro assay. results neither could inhibit association dsRNA protein. addition, 34 herbal extracts examined their inhibitory effects. Five them able electrophoresis mobility shift Four herbs, Terminalia belirica, Salacia chinensis, Zingiber montanum Peltophorum pterocarpum, reduce > 50% infectivity H5N1 cell-based assay, it is worth further studying use source drugs.