A Salmonella virulence protein that inhibits cellular trafficking.
Salmonella enterica requires a type III secretion system, designated Spi/ Ssa, to survive and proliferate within macrophages. The Spi/ Ssa system is encoded within the SPI-2 pathogenicity island and appears to function intracellularly. Here, we establish that the SPI-2-encoded SpiC protein is exported by the Spi/ Ssa type III secretion system into the host cell cytosol where it interferes with intracellular trafficking. In J774 macrophages, wild-type Salmonella inhibited fusion of Salmonella-containing phagosomes with lysosomes and endosomes, and interfered with trafficking of vesicles devoid of the microorganism. These inhibitory activities required living Salmonella and a functional spiC gene. Purified SpiC protein inhibited endosome-endosome fusion in vitro. A Sindbis virus expressing the SpiC protein interfered with normal trafficking of the transferrin receptor in vivo. A spiC mutant was attenuated for virulence, suggesting that the ability to interfere with intracellular trafficking is essential for Salmonella pathogenesis.[1]References
- A Salmonella virulence protein that inhibits cellular trafficking. Uchiya, K., Barbieri, M.A., Funato, K., Shah, A.H., Stahl, P.D., Groisman, E.A. EMBO J. (1999) [Pubmed]
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