Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix

Kaarina Lähteenmäki, Ritva Virkola, Anne Sarén, L. Emődy, Timo K. Korhonen

Research output: Contribution to journalArticle

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Abstract

The effect of the plasminogen activator Pla of Yersinia pestis on the adhesiveness of bacteria to the mammalian extracellular matrix was determined. E pestis KIM D27 harbors the 9.5-kb plasmid pPCP1, encoding Pla and pesticin; the strain efficiently adhered to the reconstituted basement membrane preparation Matrigel, to the extracellular matrix prepared from human lung NCI-H292 epithelial cells, as well as to immobilized laminin. The isogenic strain Y. pestis KIM D34 lacking pPCP1 exhibited lower adhesiveness to both matrix preparations and to laminin. Both strains showed weak adherence to type I, IV, and V collagens as well as to human plasma and cellular fibronectin. The Pla-expressing recombinant Escherichia coli LE392(pC4006) exhibited specific adhesiveness to both extracellular matrix preparations as well as to laminin. The Pla-expressing strains showed a low- affinity adherence to another basement membrane component, heparan sulfate proteoglyean, but not to chondroitin sulfate proteoglycan. The degradation of radiolabeled laminin, heparan sulfate proteoglycan, or human lung extracellular matrix by the Pla-expressing recombinant E. coli required the presence of plasminogen, and degradation was inhibited by the plasmin inhibitors aprotinin and α2-antiplasmin. Our results indicate a function of Pla in enhancing bacterial adhesion to extracellular matrices. Y. pestis also exhibits a low level of Pla-independent adhesiveness to extracellular matrices.

Original languageEnglish
Pages (from-to)5755-5762
Number of pages8
JournalInfection and Immunity
Volume66
Issue number12
Publication statusPublished - Dec 1998

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Yersinia pestis
Plasminogen Activators
Extracellular Matrix
Adhesiveness
Laminin
Antifibrinolytic Agents
Basement Membrane
Collagen Type V
Escherichia coli
Bacterial Adhesion
Chondroitin Sulfate Proteoglycans
Heparan Sulfate Proteoglycans
Lung
Aprotinin
Heparitin Sulfate
Collagen Type IV
Plasminogen
Collagen Type I
Fibronectins
Plasmids

ASJC Scopus subject areas

  • Immunology

Cite this

Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix. / Lähteenmäki, Kaarina; Virkola, Ritva; Sarén, Anne; Emődy, L.; Korhonen, Timo K.

In: Infection and Immunity, Vol. 66, No. 12, 12.1998, p. 5755-5762.

Research output: Contribution to journalArticle

Lähteenmäki, Kaarina ; Virkola, Ritva ; Sarén, Anne ; Emődy, L. ; Korhonen, Timo K. / Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix. In: Infection and Immunity. 1998 ; Vol. 66, No. 12. pp. 5755-5762.
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