ArticleThe Journal of biological chemistry2010
The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 86 citations in OpenAlex.
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- EspE3 plays a role in the pathogenicity of avian pathogenic Escherichia coli.Veterinary research · 2023Article
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- A host E3 ubiquitin ligase regulatesmLife · 2023Article
- Programmed cell death andFrontiers in microbiology · 2023Review
- Manipulation of host immune defenses by effector proteins delivered from multiple secretion systems ofFrontiers in immunology · 2023Review
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- The NEL Family of Bacterial E3 Ubiquitin Ligases.International journal of molecular sciences · 2022Review
- Insight into the Structure, Functions, and Dynamics of theMembranes · 2022Review
- Reprogramming of microRNA expression via E2F1 downregulation promotes Salmonella infection both in infected and bystander cells.Nature communications · 2021Article
- Effectors Targeting the Unfolded Protein Response during Intracellular Bacterial Infection.Microorganisms · 2021Review
- Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8.Communications biology · 2020Article
- Modification of the host ubiquitome by bacterial enzymes.Microbiological research · 2020Review
- CNS-Targeting Therapies for Lysosomal Storage Diseases: Current Advances and Challenges.Frontiers in molecular biosciences · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effectors of the type III secretion systems (T3SS) are key elements in the interaction between many Gram-negative pathogens and their hosts. SlrP is an effector that is translocated into the eukaryotic host cell through the two virulence-associated T3SS of Salmonella enterica. We found previously that this effector is an E3 ubiquitin ligase for mammalian thioredoxin. Here, we identified ERdj3, an endoplasmic reticulum lumenal chaperone of the Hsp40/DnaJ family, as a new target for SlrP. Experiments with truncated forms of ERdj3 showed that domain II was essential for the interaction with SlrP. Confocal microscopy and subcellular fractionation demonstrated that, in transfected HeLa cells, SlrP was partially located in the endoplasmic reticulum. The presence of SlrP interfered with the binding of ERdj3 to a denatured substrate. Taken together, these data suggest that the role of SlrP in the interaction between Salmonella and the host cell is exerted through the modulation of the function of two independent targets: thioredoxin in the cytosol, and ERdj3 in the endoplasmic reticulum.
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