General Information:

Id: 4,642
Diseases: Pseudomonas aeruginosa diseases
pathogen-host system
P. aeruginosa strain PA14
article
Reference: Arts IS et al.(2013) Dissecting the machinery that introduces disulfide bonds in Pseudomonas aeruginosa MBio 4 [PMID: 24327342]

Interaction Information:

Comment P. aeruginosa DsbA1 (PA14_72450), the primary donor of disulfide bonds to secreted proteins, is maintained oxidized in vivo by both DsbB1 (PA14_07000) and DsbB2 (PA14_69400). The function of DsbB1 and DsbB2 concerning the reoxidation of DsbA1 has been verified by monitoring the redox state of this oxidoreductase in dsbB1 and dsbB2 mutants. The deletion of either dsbB1 or dsbB2 does not have a significant impact on the redox state of DsbA1, however, when both DsbB proteins (DsbBs) are absent, DsbA1 accumulates mostly in the reduced form. These results indicate that both DsbB1 and DsbB2 control the redox state of DsbA1 and that both proteins are able to compensate for each other.
Formal Description
Interaction-ID: 46219

gene/protein

dsbB1

increases_activity of

gene/protein

dsbA1

only together with dsbB2 by reoxidation of dsbA1
Comment P. aeruginosa DsbA1 (PA14_72450), the primary donor of disulfide bonds to secreted proteins, is maintained oxidized in vivo by both DsbB1 (PA14_07000) and DsbB2 (PA14_69400). The function of DsbB1 and DsbB2 concerning the reoxidation of DsbA1 has been verified by monitoring the redox state of this oxidoreductase in dsbB1 and dsbB2 mutants. The deletion of either dsbB1 or dsbB2 does not have a significant impact on the redox state of DsbA1, however, when both DsbB proteins (DsbBs) are absent, DsbA1 accumulates mostly in the reduced form. These results indicate that both DsbB1 and DsbB2 control the redox state of DsbA1 and that both proteins are able to compensate for each other.
Formal Description
Interaction-ID: 46220

gene/protein

dsbB2

increases_activity of

gene/protein

dsbA1

only together with dsbB1 by reoxidation of dsbA1
Comment Deletion of both dsbB1 (PA14_07000) and dsbB2 (PA14_69400) impaired the oxidative folding of extracellular appendages and exoproteins. The authors showed that strains lacking dsbA1 (PA14_72450) or dsbB1 and dsbB2 have twitching and swimming motility defects, but not the single dsbB1 and dsbB2 mutants.
Formal Description
Interaction-ID: 46221

gene/protein

dsbA1

increases_activity of

Comment Deletion of both dsbB1 (PA14_07000) and dsbB2 (PA14_69400) impaired the oxidative folding of extracellular appendages and exoproteins. The authors showed that strains lacking dsbA1 (PA14_72450) or dsbB1 and dsbB2 have twitching and swimming motility defects, but not the single dsbB1 and dsbB2 mutant.
Formal Description
Interaction-ID: 46223

gene/protein

dsbA1

increases_activity of

Comment Both P. aeruginosa proteins DsbB1 and DsbB2 control the redox state of DsbA1 and both proteins are able to compensate for each other. The authors analyzed the roles of DsbB1 and DsbB2 in P. aeruginosa virulence in a C.elegans killing assay. Only the dsbB1B2 double mutant showed significantly less virulence than the wild-type strain but the single dsbB mutants did not show any virulence.
Formal Description
Interaction-ID: 46229

gene/protein

dsbA1

increases_activity of

process

P. aeruginosa infection

Comment The authors showed that DsbB1 (PA14_07000) and DsbB2 (PA14_69400) are both able to reoxidize DsbA1(PA14_72450) and DsbA2 (Pa14_59960).
Formal Description
Interaction-ID: 46231

gene/protein

dsbB2

increases_activity of

gene/protein

dsbA2

Comment The authors showed that DsbB1 (PA14_07000) and DsbB2 (PA14_69400) are both able to reoxidize DsbA1 (PA14_72450) and DsbA2 (Pa14_59960).
Formal Description
Interaction-ID: 46232

gene/protein

dsbB1

increases_activity of

gene/protein

dsbA2

Comment DsbA1 (PA14_72450) and DsbA2 (Pa14_59960) are both oxidoreductases, involved in P. aerugonosa disulfide bond formation system.
Formal Description
Interaction-ID: 46233

gene/protein

dsbA1

increases_activity of

Comment DsbA1 (PA14_72450) and DsbA2 (Pa14_59960) are both oxidoreductases, involved in P. aerugonosa disulfide bond formation system.
Formal Description
Interaction-ID: 46234

gene/protein

dsbA2

increases_activity of

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46235

gene/protein

dsbA1

affects_folding of

gene/protein

lasB

Drugbank entries Show/Hide entries for lasB
Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46295

gene/protein

dsbA1

affects_folding of

gene/protein

PA0572

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46301

gene/protein

dsbA1

affects_folding of

gene/protein

paaP

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46303

gene/protein

dsbA1

affects_folding of

gene/protein

cpbD

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46305

gene/protein

dsbA1

affects_folding of

gene/protein

prpL

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46308

gene/protein

dsbA1

increases_transport of

gene/protein

lasB

Drugbank entries Show/Hide entries for lasB
Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46310

gene/protein

dsbA1

increases_transport of

gene/protein

PA0572

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46311

gene/protein

dsbA1

increases_transport of

gene/protein

paaP

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46312

gene/protein

dsbA1

increases_transport of

gene/protein

cpbD

Comment The authors analyzed an oxidative protein folding system, consisting of two membrane proteins DsbB1 and DsbB2 that generate disulfide bonds de novo to deliver them to P. aeruginosa DsbA1 (PaDsbA1), a soluble oxidoreductase. PaDsbA1 in turn donates disulfide bonds to secreted proteins, including virulence factors. To analyze exoproteins affected by the impairment of the disulfide formation machinery, the authors identified five proteins that are secreted by the wild type but not by the dsbA1 and dsbB1B2 mutants. These proteins include ImpA, PaAP, CbpD, LasB, PrpL.
Formal Description
Interaction-ID: 46313

gene/protein

dsbA1

increases_transport of

gene/protein

prpL