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Related Experiment Video

Updated: Feb 2, 2026

Electroporation of Functional Bacterial Effectors into Mammalian Cells

Electroporation of Functional Bacterial Effectors into Mammalian Cells

Published on: January 19, 2015

Hsp90 Interacts with the Bacterial Effector NleH1.

Miaomiao Wu¹, Philip R Hardwidge²

¹Department of Diagnostic Medicine/Pathobiology, Kansas State University, Manhattan, KS 66506, USA. miaomiaowu@ksu.edu.

Pathogens (Basel, Switzerland)

|November 16, 2018

Summary

Enterohemorrhagic Escherichia coli (EHEC) uses NleH1 to block the NF-κB pathway by preventing RPS3 nuclear translocation. Heat shock protein 90 (Hsp90) is identified as a key cofactor in this EHEC-mediated inhibition.

Keywords:

E. coli Hsp90 NleH1 RPS3

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Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens

Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens

Published on: October 25, 2019

Area of Science:

Microbiology
Molecular Biology
Immunology

Background:

Enterohemorrhagic Escherichia coli (EHEC) employs a type III secretion system (T3SS) to deliver effector proteins into host cells.
The EHEC NleH1 effector disrupts the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) signaling pathway.
NleH1 specifically inhibits the nuclear translocation of ribosomal protein S3 (RPS3), a key component of NF-κB regulation.

Purpose of the Study:

To investigate the mechanism by which EHEC NleH1 selectively inhibits the NF-κB pathway.
To identify potential cofactors that mediate the specificity of NleH1's inhibitory action on IκB kinase-β (IKKβ) substrates.
To elucidate the role of heat shock protein 90 (Hsp90) in the interaction between IKKβ and NleH1.

Main Methods:

Investigated the interaction between EHEC NleH1, IKKβ, and Hsp90 using co-immunoprecipitation assays.
Assessed the effect of Hsp90 inhibition on RPS3 nuclear translocation in host cells infected with EHEC.
Analyzed the impact of NleH1 on IKKβ kinase activity and substrate phosphorylation.

Main Results:

Demonstrated that heat shock protein 90 (Hsp90) physically interacts with both IKKβ and the EHEC effector NleH1.
Showed that inhibition of Hsp90 activity significantly reduces the nuclear translocation of RPS3.
Confirmed that NleH1 prevents RPS3 phosphorylation by IKKβ, highlighting a specific inhibitory role.

Conclusions:

Heat shock protein 90 (Hsp90) acts as a crucial cofactor that dictates the specificity of NleH1's inhibition of the NF-κB pathway.
Targeting the Hsp90-IKKβ-NleH1 complex presents a potential strategy for therapeutic intervention against EHEC infections.
Understanding this molecular interaction provides new insights into bacterial pathogenesis and host immune evasion mechanisms.