ArticleApplied and environmental microbiology2008
DjlA, a membrane-anchored DnaJ-like protein, is required for cytotoxicity of clam pathogen Vibrio tapetis to hemocytes.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Implication of the Type IV Secretion System in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2021Article
- DnaJ molecules as potential effectors inCommunicative & integrative biology · 2019Article
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- Relation between Biofilm and Virulence in Vibrio tapetis: A Transcriptomic Study.Pathogens (Basel, Switzerland) · 2018Article
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- Article
- Screening and identification of DnaJ interaction proteins in Streptococcus pneumoniae.Current microbiology · 2013Article
- Transcriptomics of in vitro immune-stimulated hemocytes from the Manila clam Ruditapes philippinarum using high-throughput sequencing.PloS one · 2012Article
- Article
- Molecular mechanisms of ethanol-induced pathogenesis revealed by RNA-sequencing.PLoS pathogens · 2010Article
- The dawning era of comprehensive transcriptome analysis in cellular microbiology.Frontiers in microbiology · 2010Article
- 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.Antimicrobial agents and chemotherapy · 2009Article
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6 authors.
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Abstract
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 duf924(Vt), 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 djlA(Vt) but not duf924(Vt). 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.
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