ArticlePLoS pathogens2022
The Salmonella transmembrane effector SteD hijacks AP1-mediated vesicular trafficking for delivery to antigen-loading MHCII compartments.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Deletion ofFrontiers in microbiology · 2026Article
- An LPS-Deficient vaccine candidate with steD deletion confers enhanced protection against homologous and heterologous Salmonella.BMC veterinary research · 2025Article
- Bimodal expression of Type 3 Secretion System 2 enables cooperative virulence among intracellular Salmonella Typhimurium.PLoS pathogens · 2025Article
- The interplay betweenCell insight · 2025Review
- Anchorage of bacterial effector at plasma membrane via selective phosphatidic acid binding to modulate host cell signaling.PLoS pathogens · 2024Article
- Deletion of an immune evasion gene,Frontiers in immunology · 2024Article
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Manipulation of host immune defenses by effector proteins delivered from multiple secretion systems ofFrontiers in immunology · 2023Review
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
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Authors and funding
7 authors.
Funding
Abstract
SteD is a transmembrane effector of the Salmonella SPI-2 type III secretion system that inhibits T cell activation by reducing the amounts of at least three proteins -major histocompatibility complex II (MHCII), CD86 and CD97 -from the surface of antigen-presenting cells. SteD specifically localises at the trans-Golgi network (TGN) and MHCII compartments; however, the targeting, membrane integration and trafficking of SteD are not understood. Using systematic mutagenesis, we identify distinct regions of SteD that are required for these processes. We show that SteD integrates into membranes of the ER/Golgi through a two-step mechanism of membrane recruitment from the cytoplasm followed by integration. SteD then migrates to and accumulates within the TGN. From here it hijacks the host adaptor protein (AP)1-mediated trafficking pathway from the TGN to MHCII compartments. AP1 binding and post-TGN trafficking require a short sequence in the N-terminal cytoplasmic tail of SteD that resembles the AP1-interacting dileucine sorting signal, but in inverted orientation, suggesting convergent evolution.
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Registered trials
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