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Infection and Immunity, December 1998, p. 5755-5762, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Expression of Plasminogen Activator Pla of Yersinia pestis Enhances Bacterial Attachment to the Mammalian Extracellular Matrix

Kaarina Lähteenmäki,1 Ritva Virkola,1 Anne Sarén,1 Levente Emödy,2 and Timo K. Korhonen1,*

Division of General Microbiology, Department of Biosciences, FIN 00014 University of Helsinki, Finland,1 and Department of Microbiology, University Medical School, Pécs, Hungary2

Received 23 March 1998/Returned for modification 21 May 1998/Accepted 10 September 1998

The effect of the plasminogen activator Pla of Yersinia pestis on the adhesiveness of bacteria to the mammalian extracellular matrix was determined. Y. 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 proteoglycan, 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 alpha 2-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.

* Corresponding author. Mailing address: Division of General Microbiology, Department of Biosciences, P.O. Box 56, FIN 00014 University of Helsinki, Finland. Phone: 358-9-70859260. Fax: 358-9-70859262. E-mail: timo.korhonen{at}helsinki.fi.

Infection and Immunity, December 1998, p. 5755-5762, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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