DsbA of
            <i>Pseudomonas aeruginosa</i>
            Is Essential for Multiple Virulence Factors

Ha, Un-Hwan; Wang, Yanping; Jin, Shouguang

doi:10.1128/iai.71.3.1590-1595.2003

Cited by 104 publications

(108 citation statements)

References 41 publications

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“…The dsbA mutants were a kind gift from Dr. Jin (University of Florida) [36]. Bacteria lacking pili and flagellin were a kind gift from Dr. Azghani (University of Texas at Tyler).…”

Section: Mutant Strainsmentioning

confidence: 99%

Bacterial clearance of Pseudomonas aeruginosa is enhanced by the inhibition of COX‐2

et al. 2007

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Prostanoids generated by COX‐2 are involved in the regulation of inflammation but their exact role in the innate immune response has not been defined. We investigated whether COX‐2 is involved in host defense against Pseudomonas aeruginosa pneumonia. In vitro studies, in a macrophage cell line, showed that cytotoxic strain of P aeruginosa (PA103) induced significant COX‐2 protein expression and enzymatic function. In vivo data showed that infection with PA103 increased COX‐2 protein production in whole lung tissue compared to mice that were infected with mutant bacteria that lack ExoU (ΔU) or ExoU and ExoT (ΔUT). COX‐2–/– mice had accentuated clearance of cytotoxic P. aeruginosa from the lungs. We further tested the effects of COX‐2 products such as prostaglandin E2 on the function of phagocytic cells. Our studies indicate that prostaglandin E2 may be involved through interacting with the EP2 receptors in modulating the host response because treatment of macrophages with prostaglandin E2 suppressed production of reactive oxygen species. Furthermore there was enhanced bacterial clearance in EP2 receptor–/– mice compared to the wild‐type controls. Thus it is possible that inhibition of COX‐2 or EP2 receptors could be an effective adjunctive treatment for severe or resistant P. aeruginosa pneumonia.

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“…The dsbA mutants were a kind gift from Dr. Jin (University of Florida) [36]. Bacteria lacking pili and flagellin were a kind gift from Dr. Azghani (University of Texas at Tyler).…”

Section: Mutant Strainsmentioning

confidence: 99%

Bacterial clearance of Pseudomonas aeruginosa is enhanced by the inhibition of COX‐2

et al. 2007

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“…These mutants also show reduced motility because of improper assembly of the flagellum (Dailey & Berg, 1993). In pathogens, mutations in dsbA can result in decreased virulence because factors such as pili, toxins and type III secretion systems (T3SSs) require disulfide bonds to function properly (Ellermeier & Slauch, 2004;Ha et al, 2003;Jackson & Plano, 1999;Miki et al, 2004;Peek & Taylor, 1992;Watarai et al, 1995). Some Gram-negative bacteria produce DsbA and/or DsbB paralogues that either supplement or replace DsbA and DsbB activity (Grimshaw et al, 2008;Kwon & Choi, 2005;Raczko et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium

2009

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Disulfide bond formation in periplasmic proteins is catalysed by the DsbA/DsbB system in most Gram-negative bacteria. Salmonella enterica serovar Typhimurium also encodes a paralogous pair of proteins to DsbA and DsbB, DsbL and DsbI, respectively, downstream of a periplasmic arylsulfate sulfotransferase (ASST). We show that DsbL and DsbI function as a redox pair contributing to periplasmic disulfide bond formation and, as such, affect transcription of the Salmonella pathogenicity island 1 (SPI1) type three secretion system genes and activation of the RcsCDB system, as well as ASST activity. In contrast to DsbA/DsbB, however, the DsbL/DsbI system cannot catalyse the disulfide bond formation required for flagellar assembly. Phylogenic analysis suggests that the assT dsbL dsbI genes are ancestral in the Enterobacteriaceae, but have been lost in many lineages. Deletion of assT confers no virulence defect during acute Salmonella infection of mice.

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“…The locus FTT1103 is predicted to encode a hypothetical lipoprotein which shares some similarity to DsbA proteins that catalyze disulfide bond formation. The activity of DsbA has been described to be important for the formation of various virulence factors including the bacterial type IV pili biogenesis, efflux pumps and function of type III secretion system [28][29][30][31][32][33]. However, the function of the protein FTT1103 remains unknown.…”

Section: Novel Essential Virulence Factor Of F Tularensismentioning

confidence: 99%

Development of tularemic scFv antibody fragments using phage display

Kubelková

Macela

2010

Open Life Sciences

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Polyclonal antibodies, as well as monoclonal antibodies are efficacious in providing protective immunity against Francisella tularensis.This study demonstrates the application of phage display libraries for the construction of monoclonal antibodies against F. tularensis. Novel single-chain fragment variable (scFv) antibodies were generated against a whole bacterial lysate of F. tularensis live vaccine strain using the human single fold scFv libraries I (Tomlinson I + J). A total of 20 clones reacted with the bacterial cell lysate. Further, the library contains two clones responsive to recombinant lipoprotein FTT1103Δsignal (F. tularensis subsp. tularensis Schu S4), which was constructed without a signal sequence. These positively-binding scFvs were evaluated by scFv-phage enzyme-linked immunosorbent assay (ELISA). Then, positive scFvs were expressed in a soluble form in Escherichia coli HB2151 and tested for positive scFvs by using scFv-ELISA.© Versita Sp. z o.o.

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DsbA of Pseudomonas aeruginosa Is Essential for Multiple Virulence Factors

Cited by 104 publications

References 41 publications

Bacterial clearance of Pseudomonas aeruginosa is enhanced by the inhibition of COX‐2

Bacterial clearance of Pseudomonas aeruginosa is enhanced by the inhibition of COX‐2

DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium

Development of tularemic scFv antibody fragments using phage display

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