ArticleFolia microbiologica2004
alpha5beta1 integrins and fibronectin are involved in adherence of the Pseudomonas aeruginosa ER97314 clinical strain to A549 cells.
Article in Folia microbiologica, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Above the Matrix: Functional Roles for Apically Localized Integrins.Frontiers in cell and developmental biology · 2021Review
- Patient genetics is linked to chronic wound microbiome composition and healing.PLoS pathogens · 2020Article
- Microbial uptake by the respiratory epithelium: outcomes for host and pathogen.FEMS microbiology reviews · 2019Review
- The role of epithelial integrin receptors in recognition of pulmonary pathogens.Journal of innate immunity · 2009Review
- Clinical pseudomonas aeruginosa: potential factors of pathogenicity and resistance to antimicrobials.Folia microbiologica · 2006Article
- Effect of pH on production of virulence factors by biofilm cells of Pseudomonas aeruginosa.Folia microbiologica · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of fibronectin (Fn) and its natural receptors alpha5beta1 integrins in the interaction of P. aeruginosa with A549 epithelial cells was compared in the clinical isolate ER97314 and the reference PAK strain. Both strains expressed functional type IV pili, as shown by the results of the twitching motility assay. The ER97314 strain was highly adherent to immobilized Fn (640 000+/-20 000 CFU per well) while the PAK strain adhered less efficiently (70 000+/-10 000 CFU per well). Both strains adhered to A549 cells (33 400+/-1200 and 1200+/-100 CFU per well, for PAK and ER97314, respectively), only the PAK strain being significantly internalized (9430+/-2020 CFU per well). Cytochalasin D and genistein significantly decreased bacterial adherence of the 2 strains and caused also a significant decrease in PAK internalization. This inhibitory activity was not related to changes in the expression of alpha5beta1 integrins. Antibodies to Fn and alpha5beta1 integrins inhibited the adherence of the ER97314 strain but had no significant effect on PAK interaction with human cells. These findings suggest that only some P. aeruginosa strains can target Fn and their natural receptors alpha5beta1 integrins for adherence to A549 cells.
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