ArticleBMC microbiology2013
The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA.
Article in BMC microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Recent progress in molecular mechanisms of Salmonella effectors involved in gut epithelium invasion.Molecular biology reports · 2025Pooled it
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Morphogenetic penicillin-binding proteins control virulence-associated type III secretion systems inInfection and immunity · 2025Article
- Genotypic virulence profiles and associations in Salmonella isolated from meat samples in wet markets and abattoirs of Metro Manila, Philippines.BMC microbiology · 2022Article
- Analysis of In Vivo Transcriptome of Intracellular Bacterial PathogenPathogens (Basel, Switzerland) · 2021Article
- TheApplied and environmental microbiology · 2019Article
- Quantitative Yeast Genetic Interaction Profiling of Bacterial Effector Proteins Uncovers a Role for the Human Retromer in Salmonella Infection.Cell systems · 2018Article
- Article
- Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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