The C terminus of SipC binds and bundles F-actin to promote Salmonella invasion.

ABSTRACT: Salmonella enterica serovar Typhimurium invade non-phagocytic cells by injecting bacterial effector proteins to exploit the host actin cytoskeleton network. SipC is such a Salmonella effector known to nucleate actin, bundle F-actin, and translocate type III effectors. The molecular mechanism of how SipC bundles F-actin and SipC domains responsible for these activities are not well characterized. We successfully separated these activities through a series of genetic deletion/insertions in SipC. We found that the C terminus (amino acids 200-409) of SipC bundled actin filaments using in vitro biochemical assays. We further demonstrated that amino acid residues 221-260 and 381-409 of full-length SipC were indispensable for its actin binding and bundling activities. Furthermore, Salmonella muta

SUBMITTER: Myeni SK 

PROVIDER: S-EPMC2859494 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature