Proteomic characterization of novel protein-protein interactions for understanding functions of gene products

Abstract

The Yeast-Two Hybrid System is a valuable screening tool for identification and isolation of potential interacting protein partners. It is with such interest that the two important human pathogen proteins, virus coat protein 1 of Enterovirus 71 and U95 of Human Herpesvirus 6, were selected as baits in this research. We demonstrated binding affinity between VP1 and three human proteins, ornithine decarboxylase (ODC1), gene trap ankyrin repeat (GTAR), and KIAA0697. Similarly, the Immediate-Early gene, U95, demonstrated binding affinity for GRIM-19. All interactions were authenticated by both co-immunoprecipitation and co-immunolocalization experiments. These viral-host protein interactions may provide insights into the role of structural and Immediate-Early proteins in the pathogenesis of viral diseases.