Author/Authors :
Shinya Oishi، نويسنده , , Yasuyo Kodera، نويسنده , , Hiroki Nishikawa، نويسنده , , Hirotaka Kamitani، نويسنده , , Tsuyoshi Watabe، نويسنده , , Hiroaki Ohno، نويسنده , , Tadafumi Tochikura، نويسنده , , Kazuki Shimane، نويسنده , , Eiichi Kodama، نويسنده , , Masao Matsuoka، نويسنده , , Fuminori Mizukoshi، نويسنده , , Hajime Tsujimoto، نويسنده , , Nobutaka Fujii*، نويسنده ,
Abstract :
Feline immunodeficiency virus (FIV) is a pathogenic virus that causes an AIDS-like syndrome in the domestic cats. For viral entry and infection, fusion between the virus and the cell membrane is the critical process and this process is mediated by an envelope glycoprotein gp40. We have identified fusion inhibitory peptides from the heptad repeat-2 (HR2) of gp40. Remodeling of the original sequences using α-helix-inducible motifs revealed the interactive residues of gp40. Comparative analysis of HR2 peptides derived from four FIV strains demonstrated that the interactive surface of the Shizuoka strain-derived HR2 peptides provides the highest affinity of all the FIV strains examined.
Keywords :
Fusion inhibitor , ?-Helix , Heptad repeat , Feline immunodeficiency virus