Document Detail

The Salmonella type III secretion effector, salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3.
MedLine Citation:
PMID:  20335166     Owner:  NLM     Status:  MEDLINE    
Effectors of the type III secretion systems (T3SS) are key elements in the interaction between many Gram-negative pathogens and their hosts. SlrP is an effector that is translocated into the eukaryotic host cell through the two virulence-associated T3SS of Salmonella enterica. We found previously that this effector is an E3 ubiquitin ligase for mammalian thioredoxin. Here, we identified ERdj3, an endoplasmic reticulum lumenal chaperone of the Hsp40/DnaJ family, as a new target for SlrP. Experiments with truncated forms of ERdj3 showed that domain II was essential for the interaction with SlrP. Confocal microscopy and subcellular fractionation demonstrated that, in transfected HeLa cells, SlrP was partially located in the endoplasmic reticulum. The presence of SlrP interfered with the binding of ERdj3 to a denatured substrate. Taken together, these data suggest that the role of SlrP in the interaction between Salmonella and the host cell is exerted through the modulation of the function of two independent targets: thioredoxin in the cytosol, and ERdj3 in the endoplasmic reticulum.
Joaquín Bernal-Bayard; Elena Cardenal-Muñoz; Francisco Ramos-Morales
Related Documents :
19430636 - Brazilian contribution for a better knowledge on the biology of toxoplasma gondii.
7957756 - In vitro development of infectious liver stages of p. yoelii and p. berghei malaria in ...
11295456 - Are the actively respiring cells (ctc+) those responsible for bacterial production in a...
19061866 - Arf6, pi3-kinase and host cell actin cytoskeleton in toxoplasma gondii cell invasion.
21235616 - Effects of enamel matrix derivative on periodontal wound healing in an inflammatory env...
22008306 - Selenium inhibits migration of murine melanoma cells via down-modulation of il-18 expre...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-24
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-05-17     Completed Date:  2010-06-14     Revised Date:  2011-07-28    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16360-8     Citation Subset:  IM    
Departamento de Genética, Facultad de Biología, Universidad de Sevilla, Apartado 1095, 41080 Sevilla, Spain.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Bacterial Proteins / genetics,  metabolism*
Endoplasmic Reticulum / genetics,  metabolism
HSP40 Heat-Shock Proteins / genetics,  metabolism*
Hela Cells
Protein Binding
Protein Structure, Tertiary
Salmonella typhimurium / genetics,  metabolism*,  pathogenicity
Thioredoxins / genetics,  metabolism
Ubiquitin-Protein Ligases / genetics,  metabolism*
Reg. No./Substance:
0/Bacterial Proteins; 0/DNAJB11 protein, human; 0/HSP40 Heat-Shock Proteins; 0/SlrP protein, Salmonella typhimurium; 52500-60-4/Thioredoxins; EC Ligases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Transmembrane segment 11 appears to line the purine permeation pathway of the Plasmodium falciparum ...
Next Document:  Stability of the LATS2 tumor suppressor gene is regulated by tristetraprolin.