alpha5beta1 integrins and fibronectin are involved in adherence of the Pseudomonas aeruginosa ER97314 clinical strain to A549 cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
15881415
DOI
10.1007/bf02931561
Knihovny.cz E-zdroje
- MeSH
- bakteriální adheze * MeSH
- buněčné linie MeSH
- epitelové buňky mikrobiologie MeSH
- fibronektiny metabolismus MeSH
- integrin alfa5beta1 metabolismus MeSH
- lidé MeSH
- Pseudomonas aeruginosa patogenita fyziologie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fibronektiny MeSH
- integrin alfa5beta1 MeSH
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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J Bacteriol. 2001 Jan;183(2):763-7 PubMed
Curr Opin Microbiol. 2002 Feb;5(1):81-6 PubMed
Microb Pathog. 2002 Sep;33(3):135-43 PubMed
Infect Immun. 1999 Jul;67(7):3207-14 PubMed
Microb Pathog. 2002 Sep;33(3):109-14 PubMed
Infect Immun. 2001 Jan;69(1):281-7 PubMed
Chemotherapy. 2001 Sep-Oct;47(5):344-9 PubMed
Infect Immun. 1991 Mar;59(3):822-8 PubMed
Folia Microbiol (Praha). 1992;37(2):140-5 PubMed
Infect Immun. 1996 Jun;64(6):2288-94 PubMed
Microbes Infect. 2000 Jul;2(9):1051-60 PubMed
Microbes Infect. 2002 May;4(6):613-20 PubMed
Matrix Biol. 1999 Jun;18(3):211-23 PubMed
Exp Cell Res. 1994 Jan;210(1):113-22 PubMed
J Cell Biol. 1992 Jan;116(2):477-87 PubMed
Infect Immun. 1994 Dec;62(12):5456-63 PubMed
Protein Expr Purif. 1999 Oct;17(1):146-52 PubMed
Infect Immun. 1995 Oct;63(10):4072-7 PubMed
Gene. 1997 Jun 11;192(1):99-108 PubMed
C R Acad Sci III. 1999 Dec;322(12):1071-80 PubMed
FEMS Microbiol Lett. 2002 Jul 16;213(1):73-9 PubMed
Eur Respir J. 1999 Jun;13(6):1301-9 PubMed
Microbes Infect. 2000 Jun;2(7):793-801 PubMed
Int J Cancer. 1999 Jan 18;80(2):285-94 PubMed
Infect Immun. 1997 Jul;65(7):2861-7 PubMed
Am J Respir Crit Care Med. 1996 Oct;154(4 Pt 2):S155-62 PubMed
