Study On Proteins Interacting With Invasion Plasmid Antigen C Of Shigella Flexneri 2a

Bacillary dysentery is a severe infectious disease all over the world and still a threat to human health and life. The pathogens of this disease belong to Gram-negative Shigella, the family Enterobacteriaceae. Of the four sorts of Shigella, S. flexneri is mainly responsible for the endemic form of bacillary dysentery in our country. It is a facultative intracellular bacterial pathogen that invades human colonic epithelial cells by a process called pathogen-induced phagocytosis. The ipa (invasion plasmid antigen) operon in the large virulence plasmid of S. flexneri is necessary to encode and secrete invasion plasmid antigen proteins. It encodes four secreted proteins: IpaB, IpaC, IpaD and IpaA. Ipa proteins are rapidly secreted from S. flexneri when the bacterium comes into contact with epithelial cells. Following their secretion, IpaB and IpaC are found as part of a protein complex and this complex is absolutely required for pathogen entry into epithelial cells. Previous work has shown that exogenously added recombinant IpaC is sufficient for promoting the uptake of S. flexneri, indicating that IpaC plays an important role in the pathogenicity of this pathogen. In order to further understand the roles of the IpaC proteins in the pathogenesis of shigellosis, it is an advisable strategy to isolate proteins that potentially interact with Ipa proteins in host cells. The two-hybrid system is an effective genetic method to identify protein-protein interaction, so a two-hybrid system has been exploited to identify of IpaC-interacting protein in host cells. There is no similar domestic and abroad report in this field.