Hsp90 Interacts with the Bacterial Effector NleH1

Hsp90 Interacts with the Bacterial Effector NleH1

Enterohemorrhagic <i>Escherichia coli</i> (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-&#954;B) pathway by reducing the nuclear t...

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Bibliographic Details
Main Authors: Miaomiao Wu, Philip R. Hardwidge
Format: Article
Language:English
Published: MDPI AG 2018-11-01
Series:Pathogens
Subjects:
<i>E. coli</i>
Hsp90
NleH1
RPS3
Online Access:https://www.mdpi.com/2076-0817/7/4/87
Description
Summary:Enterohemorrhagic <i>Escherichia coli</i> (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-&#954;B) pathway by reducing the nuclear translocation of the ribosomal protein S3 (RPS3). NleH1 prevents RPS3 phosphorylation by the I&#954;B kinase-&#946; (IKK&#946;). IKK&#946; is a central kinase in the NF-&#954;B pathway, yet NleH1 only restricts the phosphorylation of a subset of the IKK&#946; substrates. We hypothesized that a protein cofactor might dictate this inhibitory specificity. We determined that heat shock protein 90 (Hsp90) interacts with both IKK&#946; and NleH1 and that inhibiting Hsp90 activity reduces RPS3 nuclear translocation.
ISSN:2076-0817

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