Abstract
BackgroundSalmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever. This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate cellular function. Salmonella pathogenicity island (SPI)-2 encodes a T3SS required for intracellular survival of the pathogen. Genes in SPI-2 include apparatus components, secreted effectors and chaperones that bind to secreted cargo to coordinate their release from the bacterial cell. Although the effector repertoire secreted by the SPI-2 T3SS is large, only three virulence-associated chaperones have been characterized.ResultsHere we report that SscA is the chaperone for the SseC translocon component. We show that SscA and SseC interact in bacterial cells and that deletion of sscA results in a loss of SseC secretion, which compromises intracellular replication and leads to a loss of competitive fitness in mice.ConclusionsThis work completes the characterization of the chaperone complement within SPI-2 and identifies SscA as the chaperone for the SseC translocon.
Highlights
Salmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever
Typhimurium) has two Type 3 secretion system (T3SS) encoded within Salmonella pathogenicity island-1 (SPI-1) and SPI-2 that facilitate invasion and intracellular survival within host cells [1,2,3]
Three virulence chaperones have been characterized; we showed that SrcA chaperones the effectors SseL and PipB2 and binds to the T3SS ATPase SsaN [5]
Summary
Salmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate cellular function. Bacterial pathogens exploit host niches using strategies that block or modify host defense pathways One such strategy employed by the Gram-negative bacterium Salmonella enterica, is the translocation of effector proteins into the host cell through a type three secretion system (T3SS). The assembly of the T3SS is complex, involving the formation of membrane channels in the bacterial inner and outer membrane, and a terminal translocon that forms a pore in host membranes Both SPI-1 and SPI-2 encode a distinct group of chaperones that bind to their cognate cargo proteins to
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