ArticleMicrobiology (Reading, England)2019
SrcA is a chaperone for the Salmonella SPI-2 type three secretion system effector SteD.
Article in Microbiology (Reading, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Oral administration of probiotic spores-based biohybrid system for efficient attenuation of Salmonella Typhimurium-induced colitis.Journal of nanobiotechnology · 2025Article
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- The Salmonella transmembrane effector SteD hijacks AP1-mediated vesicular trafficking for delivery to antigen-loading MHCII compartments.PLoS pathogens · 2022Article
- Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens.Veterinary research · 2021Review
- Co-occurrence ofInfection and drug resistance · 2021Article
- The Tumour Suppressor TMEM127 Is a Nedd4-Family E3 Ligase Adaptor Required by Salmonella SteD to Ubiquitinate and Degrade MHC Class II Molecules.Cell host & microbe · 2020Article
- Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Effector proteins of type three secretion systems (T3SS) often require cytosolic chaperones for their stabilization, to interact with the secretion machinery and to enable effector delivery into host cells. We found that deletion of srcA, previously shown to encode a chaperone for the Salmonella pathogenicity island 2 (SPI-2) T3SS effectors SseL and PipB2, prevented the reduction of mature Major Histocompatibility Complex class II (mMHCII) from the surface of antigen-presenting cells during Salmonella infection. This activity was shown previously to be caused by the SPI-2 T3SS effector SteD. Since srcA and steD are located in the same operon on the Salmonella chromosome, this suggested that the srcA phenotype might be due to an indirect effect on SteD. We found that SrcA is not translocated by the SPI-2 T3SS but interacts directly and forms a stable complex with SteD in bacteria with a 2 : 1 stoichiometry. We found that SrcA was not required for SPI-2 T3SS-dependent, neutral pH-induced secretion of either SseL or PipB2 but was essential for secretion of SteD. SrcA therefore functions as a chaperone for SteD, explaining its requirement for the reduction in surface levels of mMHCII.
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