2005
An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates
Li L, Ledizet M, Kar K, Koski RA, Kazmierczak BI. An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates. Annals Of Clinical Microbiology And Antimicrobials 2005, 4: 22. PMID: 16375761, PMCID: PMC1360672, DOI: 10.1186/1476-0711-4-22.Peer-Reviewed Original ResearchConceptsClinical isolatesEpithelial cellsOptimal treatment strategyLarge clinical studiesP. aeruginosa type III secretion systemP. aeruginosa isolatesEnzyme-linked immunosorbent assayEnzyme-linked immunosorbentType III secretion systemSecretion phenotypeIndirect enzyme-linked immunosorbentPseudomonas aeruginosaPoor outcomeInfected patientsIndirect enzyme-linked immunosorbent assayTreatment strategiesClinical studiesClinical diseaseSevere diseaseAeruginosa isolatesELISA assaysConclusionThe availabilityImmunosorbent assayCultured epithelial cellsVirulence factors
2003
Epithelial Cell Polarity Alters Rho-GTPase Responses to Pseudomonas aeruginosa
Kazmierczak BI, Mostov K, Engel JN. Epithelial Cell Polarity Alters Rho-GTPase Responses to Pseudomonas aeruginosa. Molecular Biology Of The Cell 2003, 15: 411-419. PMID: 14595106, PMCID: PMC329196, DOI: 10.1091/mbc.e03-08-0559.Peer-Reviewed Original ResearchConceptsRho family GTPasesPolarized MDCK monolayersActin polymerizationP. aeruginosa entryRho family GTPase activationMDCK monolayersCdc42-GTP levelsClostridium difficile toxin BOpportunistic human pathogenMadin-Darby canine kidney cellsActivation of RhoAEpithelial cellsDifficile toxin BCanine kidney cellsCell polarityBasolateral infectionMDCK cell monolayersGTPase activationDifferentiation stateP. aeruginosaPseudomonas aeruginosaSurface proteinsBasolateral surfaceHuman pathogensGTPases
2002
Pseudomonas aeruginosa ExoT Acts In Vivo as a GTPase-Activating Protein for RhoA, Rac1, and Cdc42
Kazmierczak B, Engel J. Pseudomonas aeruginosa ExoT Acts In Vivo as a GTPase-Activating Protein for RhoA, Rac1, and Cdc42. Infection And Immunity 2002, 70: 2198-2205. PMID: 11895987, PMCID: PMC127837, DOI: 10.1128/iai.70.4.2198-2205.2002.Peer-Reviewed Original Research
2001
INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM
Kazmierczak B, Mostov K, Engel J. INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM. Annual Review Of Microbiology 2001, 55: 407-435. PMID: 11544362, DOI: 10.1146/annurev.micro.55.1.407.Peer-Reviewed Original ResearchPseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair
Geiser T, Kazmierczak B, Garrity‐Ryan L, Matthay M, Engel J. Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair. Cellular Microbiology 2001, 3: 223-236. PMID: 11298646, DOI: 10.1046/j.1462-5822.2001.00107.x.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsEpithelial wound repairPseudomonas aeruginosa ExoTRho family GTPasesWound repairPathogen Pseudomonas aeruginosaNosocomial pathogen Pseudomonas aeruginosaP. aeruginosa internalizationEpithelial cellsP. aeruginosaGAP domainGAP activityBacterial proteinsCell roundingCytoskeleton collapseLung epithelial wound repairExoTCell detachmentVivo virulenceProteinEpithelial tissue damageImmune effector cellsLocal host defenseIntact epithelial barrierHost defenseRho GTPase activity modulates Pseudomonas aeruginosa internalization by epithelial cells
Kazmierczak B, Jou T, Mostov K, Engel J. Rho GTPase activity modulates Pseudomonas aeruginosa internalization by epithelial cells. Cellular Microbiology 2001, 3: 85-98. PMID: 11207623, DOI: 10.1046/j.1462-5822.2001.00091.x.Peer-Reviewed Original ResearchConceptsRho-GTP levelsP. aeruginosa internalizationRho familyEpithelial cellsGTP levelsRho-specific inhibitorRho family GTPasesC3 ADP-ribosyltransferaseRho GTPase activityPathogen Pseudomonas aeruginosaGram-negative pathogen Pseudomonas aeruginosaMadin-Darby canine kidney cellsPseudomonas aeruginosa internalizationCanine kidney cellsNative RhoActive alleleBacterial internalizationGTPase activityP. aeruginosa strain PA103Fusion constructsADP-ribosyltransferaseLatrunculin A.Active Rac1Bacterial uptakeHeLa cells
2000
The Arginine Finger Domain of ExoT Contributes to Actin Cytoskeleton Disruption and Inhibition of Internalization ofPseudomonas aeruginosa by Epithelial Cells and Macrophages
Garrity-Ryan L, Kazmierczak B, Kowal R, Comolli J, Hauser A, Engel J. The Arginine Finger Domain of ExoT Contributes to Actin Cytoskeleton Disruption and Inhibition of Internalization ofPseudomonas aeruginosa by Epithelial Cells and Macrophages. Infection And Immunity 2000, 68: 7100-7113. PMID: 11083836, PMCID: PMC97821, DOI: 10.1128/iai.68.12.7100-7113.2000.Peer-Reviewed Original ResearchConceptsEpithelial cellsImportant nosocomial pathogenType III secretion systemHost cellsMacrophage-like cellsAcute pneumoniaMouse modelNosocomial pathogenOfPseudomonas aeruginosaType IIIJ774.1 macrophage-like cellsSecretion systemStrain PA103ExoTPseudomonas aeruginosaCellsCytoskeleton disruptionNegative regulatorPA103Reduced colonizationActin cytoskeleton disruptionPrevious studiesAeruginosaPneumoniaVirulence