ArticleInfection and immunity2010
Delineation of regions of the Yersinia YopM protein required for interaction with the RSK1 and PRK2 host kinases and their requirement for interleukin-10 production and virulence.
Article in Infection and immunity, 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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Who cites it
50 citing papers in PubMed, 80 citations in OpenAlex.
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- A case of convergent evolution: Several viral and bacterial pathogens hijack RSK kinases through a common linear motif.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host.Nature communications · 2022Article
- Role of the Yersinia pseudotuberculosis Virulence Plasmid in Pathogen-Phagocyte Interactions in Mesenteric Lymph Nodes.EcoSal Plus · 2021Review
- γδ T cell IFNγ production is directly subverted by Yersinia pseudotuberculosis outer protein YopJ in mice and humans.PLoS pathogens · 2021Article
- The structure and function of protein kinase C-related kinases (PRKs).Biochemical Society transactions · 2021Review
- Bacterial nucleomodulins: A coevolutionary adaptation to the eukaryotic command center.PLoS pathogens · 2021Review
- The pyrin inflammasome and the Yersinia effector interaction.Immunological reviews · 2020Review
- Ancient familial Mediterranean fever mutations in human pyrin and resistance to Yersinia pestis.Nature immunology · 2020Article
- The pyrin inflammasome in host-microbe interactions.Current opinion in microbiology · 2020Review
- Review
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- Chromosomally-EncodedFrontiers in cellular and infection microbiology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The YopM protein of Yersinia sp. is a type III secreted effector that is required for virulence in murine models of infection. YopM has previously been shown to contain leucine-rich repeats (LRRs) and to interact with two host kinases, RSK1 and PRK2, although the consequence of these interactions is unknown. A series of YopM proteins missing different numbers of LRRs or a C-terminal domain were produced and used for in vitro binding reactions to map domains required for interaction with RSK1 and PRK2. A C-terminal domain of YopM (from LRR12 to the C terminus) was shown to be required for interaction with RSK1, while an internal portion encompassing LRR6 to LRR15 was shown to be required for interaction with PRK2. The virulence of a Yersinia pseudotuberculosis Delta yopM mutant in mice via an intravenous route of infection was significantly attenuated. At day 4 postinfection, there were significantly increased levels of gamma interferon and reduced levels of interleukin-18 (IL-18) and IL-10 in the serum of the Delta yopM-infected mice compared to that of mice infected with the wild type, suggesting that YopM action alters the balance of these key cytokines to promote virulence. The PRK2 and RSK1 interaction domains of YopM were both required for IL-10 induction in vivo, irrespective of splenic colonization levels. In an orogastric model of Y. pseudotuberculosis infection, a Delta yopM mutant was defective in dissemination from the intestine to the spleen and significantly reduced in virulence. In addition, Y. pseudotuberculosis mutants expressing YopM proteins unable to interact with either RSK1 (YopM Delta 12-C) or PRK2 (YopM Delta 6-15) were defective for virulence in this assay, indicating that both interaction domains are important for YopM to promote pathogenesis.
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