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
Pseudomonas 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 defense
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