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SseL Deubiquitinates RPS3 to Inhibit Its Nuclear Translocation
Open AccessArticle

Hsp90 Interacts with the Bacterial Effector NleH1

Department of Diagnostic Medicine/Pathobiology, Kansas State University, Manhattan, KS 66506, USA
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Author to whom correspondence should be addressed.
Pathogens 2018, 7(4), 87; https://doi.org/10.3390/pathogens7040087
Received: 26 September 2018 / Revised: 31 October 2018 / Accepted: 11 November 2018 / Published: 13 November 2018
Enterohemorrhagic Escherichia coli (EHEC) utilizes a type III secretion system (T3SS) to inject effector proteins into host cells. The EHEC NleH1 effector inhibits the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) pathway by reducing the nuclear translocation of the ribosomal protein S3 (RPS3). NleH1 prevents RPS3 phosphorylation by the IκB kinase-β (IKKβ). IKKβ is a central kinase in the NF-κB pathway, yet NleH1 only restricts the phosphorylation of a subset of the IKKβ substrates. We hypothesized that a protein cofactor might dictate this inhibitory specificity. We determined that heat shock protein 90 (Hsp90) interacts with both IKKβ and NleH1 and that inhibiting Hsp90 activity reduces RPS3 nuclear translocation. View Full-Text
Keywords: E. coli; Hsp90; NleH1; RPS3 E. coli; Hsp90; NleH1; RPS3
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Wu, M.; Hardwidge, P.R. Hsp90 Interacts with the Bacterial Effector NleH1. Pathogens 2018, 7, 87.

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