This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lakhal, F.
Right arrow Articles by Jacq, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lakhal, F.
Right arrow Articles by Jacq, A.
Agricola
Right arrow Articles by Lakhal, F.
Right arrow Articles by Jacq, A.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, September 2008, p. 5750-5758, Vol. 74, No. 18
0099-2240/08/$08.00+0     doi:10.1128/AEM.01043-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

DjlA, a Membrane-Anchored DnaJ-Like Protein, Is Required for Cytotoxicity of Clam Pathogen Vibrio tapetis to Hemocytes{triangledown}

Fatma Lakhal,1 Stéphanie Bury-Moné,1,{dagger} Yanoura Nomane,1 Nelly Le Goïc,2 Christine Paillard,2 and Annick Jacq1*

Institut de Génétique et Microbiologie, UMR8621, CNRS, Université Paris-Sud XI, Bâtiment 400, Centre Scientifique d'Orsay, 91405 Orsay Cedex, France,1 LEMAR, UMR 6539, CNRS, Institut Universitaire Européen de la Mer, Université de Bretagne Occidentale, Technopole Brest-Iroise, Place Copernic, 29280 Plouzané, France2

Received 9 May 2008/ Accepted 11 July 2008

DjlA is an inner membrane cochaperone belonging to the DnaJ family, which has been shown to be involved in Legionella sp. pathogenesis. In this study, we explored the role of this protein in the physiology and virulence of Vibrio tapetis, the etiological agent of brown ring disease (BRD) in Manila clam (Ruditapes philippinarum). Analysis of the djlA locus in V. tapetis revealed a putative organization in an operon with a downstream gene that we designated duf924Vt, which encodes a conserved protein with an unknown function and has homologues in bacteria and eukaryotes. djlA mutants displayed a reduced growth rate and showed an important loss of cytotoxic activity against R. philippinarum hemocytes in vitro, which could be restored by extrachromosomal expression of wild-type djlAVt but not duf924Vt. These results are in keeping with the potential importance of DjlA for bacterial pathogenicity and open new perspectives for understanding the mechanism of action of this protein in the novel V. tapetis-R. philippinarum interaction model.


* Corresponding author. Mailing address: Institut de Génétique et Microbiologie, Bâtiment 400, Université Paris-Sud, Orsay 91405 Cedex, France. Phone: 33-1 69 15 57 17. Fax: 33-1 69 15 66 78. E-mail: annick.jacq{at}igmors.u-psud.fr

{triangledown} Published ahead of print on 18 July 2008.

{dagger} Present address: LBPA, CNRS-UMR 8113, E.N.S. Cachan, 61 avenue du Président Wilson, 94235 Cachan, France.


Applied and Environmental Microbiology, September 2008, p. 5750-5758, Vol. 74, No. 18
0099-2240/08/$08.00+0     doi:10.1128/AEM.01043-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Moran-Barrio, J., Limansky, A. S., Viale, A. M. (2009). Secretion of GOB Metallo-{beta}-Lactamase in Escherichia coli Depends Strictly on the Cooperation between the Cytoplasmic DnaK Chaperone System and the Sec Machinery: Completion of Folding and Zn(II) Ion Acquisition Occur in the Bacterial Periplasm. Antimicrob. Agents Chemother. 53: 2908-2917 [Abstract] [Full Text]