Next Article in Journal
Hsp90 Interacts with the Bacterial Effector NleH1
Previous Article in Journal
Pathotypes of Xanthomonas axonopodis pv. dieffenbachiae Isolated from Anthurium andraeanum in China
Article Menu

Export Article

Open AccessArticle
Pathogens 2018, 7(4), 86;

SseL Deubiquitinates RPS3 to Inhibit Its Nuclear Translocation

Department of Diagnostic Medicine/Pathobiology, Kansas State University, Manhattan, KS 66506, USA
Author to whom correspondence should be addressed.
Received: 23 September 2018 / Revised: 2 November 2018 / Accepted: 5 November 2018 / Published: 7 November 2018
Full-Text   |   PDF [2535 KB, uploaded 7 November 2018]   |  


Many Gram-negative bacterial pathogens use type III secretion systems to deliver virulence proteins (effectors) into host cells to counteract innate immunity. The ribosomal protein S3 (RPS3) guides NF-κB subunits to specific κB sites and plays an important role in the innate response to bacterial infection. Two E. coli effectors inhibit RPS3 nuclear translocation. NleH1 inhibits RPS3 phosphorylation by IKK-β, an essential aspect of the RPS3 nuclear translocation process. NleC proteolysis of p65 generates an N-terminal p65 fragment that competes for full-length p65 binding to RPS3, thus also inhibiting RPS3 nuclear translocation. Thus, E. coli has multiple mechanisms by which to block RPS3-mediated transcriptional activation. With this in mind, we considered whether other enteric pathogens also encode T3SS effectors that impact this important host regulatory pathway. Here we report that the Salmonella Secreted Effector L (SseL), which was previously shown to function as a deubiquitinase and inhibit NF-κB signaling, also inhibits RPS3 nuclear translocation by deubiquitinating this important host transcriptional co-factor. RPS3 deubiquitination by SseL was restricted to K63-linkages and mutating the active-site cysteine of SseL abolished its ability to deubiquitinate and subsequently inhibit RPS3 nuclear translocation. Thus, Salmonella also encodes at least one T3SS effector that alters RPS3 activities in the host nucleus. View Full-Text
Keywords: effector; nuclear translocation; RSP3; SseL; ubiquitination effector; nuclear translocation; RSP3; SseL; ubiquitination

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Wu, M.; El Qaidi, S.; Hardwidge, P.R. SseL Deubiquitinates RPS3 to Inhibit Its Nuclear Translocation. Pathogens 2018, 7, 86.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Pathogens EISSN 2076-0817 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top