Pseudomonas aeruginosa invasion of and multiplication within corneal epithelial cells in vitro

Fleiszig, Suzanne M. J.; Zaidi, Tanweer; Pier, Gerald B.

doi:10.1128/iai.63.10.4072-4077.1995

Cited by 166 publications

(96 citation statements)

References 14 publications

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“…Previous studies have shown that actin cytoskeleton disruption mediated via toxins such as cytochalasin D or latrunculin A or other TTSS effectors, e.g., ExoT and ExoS has significant invasion-inhibitory activity towards P. aeruginosa [7,30,[36][37][38]. Consistent with those earlier studies, ExoY-mediated actin disruption at 2 h coincided with inhibition of bacterial invasion for both adenylate cyclase active and inactive forms of the molecule.…”

Section: Discussionsupporting

confidence: 86%

Actin cytoskeleton disruption by ExoY and its effects onPseudomonas aeruginosainvasion

Cowell

Evans

Fleiszig

2005

FEMS Microbiology Letters

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Three of the Type III-secreted effectors of Pseudomonas aeruginosa (ExoS, ExoT, and ExoY) each alter mammalian cell morphology in culture without causing a loss of cell viability. For ExoS and ExoT this property involves RhoGAP activity, and leads to actin cytoskeleton disruption and a reduced capacity for internalizing bacteria. ExoY does not possess RhoGAP activity. Instead, cell rounding depends upon its adenylate cyclase catalytic region. Since anti-phagocytic activities of ExoS and ExoT are associated with cell rounding and cytoskeleton disruption, we hypothesized that ExoY would also inhibit P. aeruginosa invasion of epithelial cells coinciding with adenylate cyclase-mediated cytoskeleton disruption. The results showed actin disruption of epithelial cells at 2 h post-infection associated with both adenylate cyclase-active ExoY and its catalytic mutant form ExoYK81M, and which coincided with inhibition of bacterial invasion (76% inhibition by ExoY, and 37% by ExoYK81M). Surprisingly, at 4h post-infection, neither form of ExoY inhibited invasion despite extensive actin disruption. These data suggest that ExoY, like ExoS and ExoT, contains more than one active domain affecting mammalian cell function. The data also suggest that cytoskeleton disruption does not necessarily predict invasion inhibitory activity, supporting the recently proposed model that P. aeruginosa internalization can proceed through more than one pathway.

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Section: Discussionsupporting

confidence: 86%

Actin cytoskeleton disruption by ExoY and its effects onPseudomonas aeruginosainvasion

Cowell

Evans

Fleiszig

2005

FEMS Microbiology Letters

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“…Among the compounds acting on cytoskeletal structures, cytochalasins can prevent the uptake of microorganisms or inhibit intracellular bacterial multiplication (1. 3,4,10,12,15,16,28). An inhibiting effect on L. pneumophila internalisation in Acanthamoeba castellanii was reported by Moffat and Tompkins (23).…”

Section: Discussionmentioning

confidence: 81%

Multiplication of Legionella pneumophila in HeLa Cells in the Presence of Cytoskeleton and Metabolic Inhibitors

Goldoni

Cattani

Carrara

et al. 1998

Microbiology and Immunology

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A study has been carried out on the action of cytoskeleton and metabolic inhibitors on intracellular multiplication in HeLa cells of a virulent strain of Legionella pneumophila serogroup 6. The effects of the substances were separately tested on both penetration and intracellular multiplication of L. pneumophila. Only cytochalasin A and 2-deoxy-D-glucose (2dG) affected bacterial internalisation, whereas intracellular multiplication was inhibited by cytochalasins A, B, C, D and J (D being the most active) and by 2dG with a dose-response effect. The action of 2dG was counteracted by 50 mm glucose. Experiments carried out with cytochalasin D and a rhodamine-phalloidin conjugate showed the involvement of cytoskeletal elements in intracellular multiplication of Legionella; compounds acting on microtubules had no effect.

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“…These were used to quantify the extent of bacterial invasion of HeLa cells. These assays were performed as described previously for assessing Pseudomonas aeruginosa invasion of epithelial cells (Fleiszig et al, 1995).…”

Section: Cell Infectionmentioning

confidence: 99%

Identification of Brucella spp. genes involved in intracellular trafficking

et al. 2001

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SummaryAfter uptake by host cells, the pathogen Brucella transits through early endosomes, evades phago± lysosome fusion and replicates in a compartment associated with the endoplasmic reticulum (ER). The molecular mechanisms underlying these processes are still poorly understood. To identify new bacterial factors involved in these processes, a library of 1800 Brucella melitensis 16M mini-Tn5catkm mutants was screened for intracellular survival and multiplication in HeLa cells and J774A.1 macrophages. Thirteen mutants were identified as defective for their intracellular survival in both cell types. In 12 of them, the transposon had inserted in the virB operon, which encodes a type IV-related secretion system. The preponderance of virB mutants demonstrates the importance of this secretion apparatus in the intracellular multiplication of B. melitensis. We also examined the intracellular fate of three virB mutants (virB2, virB4 and virB9) in HeLa cells by immunofluorescence. The three VirB proteins are not necessary for penetration and the inhibition of phago±lysosomal fusion within non-professional phagocytes. Rather, the virB mutants are unable to reach the replicative niche and reside in a membranebound vacuole expressing the late endosomal marker, LAMP1, and the sec61b protein from the ER membrane, proteins that are present in autophagic vesicles originating from the ER.

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Pseudomonas aeruginosa invasion of and multiplication within corneal epithelial cells in vitro

Cited by 166 publications

References 14 publications

Actin cytoskeleton disruption by ExoY and its effects onPseudomonas aeruginosainvasion

Actin cytoskeleton disruption by ExoY and its effects onPseudomonas aeruginosainvasion

Multiplication of Legionella pneumophila in HeLa Cells in the Presence of Cytoskeleton and Metabolic Inhibitors

Identification of Brucella spp. genes involved in intracellular trafficking

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