Expression of Plasminogen Activator Pla of Yersinia pestis Enhances Bacterial Attachment to the Mammalian Extracellular Matrix
| Autor: | Levente Emödy, Kaarina Lähteenmäki, Ritva Virkola, Timo K. Korhonen, Anne Sarén |
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| Rok vydání: | 1998 |
| Předmět: |
Yersinia pestis
Immunology In Vitro Techniques Microbiology Bacterial Adhesion Basement Membrane Extracellular matrix Plasminogen Activators 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Laminin Escherichia coli medicine Extracellular Humans Lung 030304 developmental biology Basement membrane 0303 health sciences biology 030306 microbiology Epithelial Cells respiratory system Molecular biology Recombinant Proteins Extracellular Matrix Fibronectin Drug Combinations Infectious Diseases medicine.anatomical_structure Proteoglycan chemistry Chondroitin sulfate proteoglycan Molecular and Cellular Pathogenesis biology.protein Proteoglycans Parasitology Collagen Plasminogen activator |
| Zdroj: | Infection and Immunity. 66:5755-5762 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.66.12.5755-5762.1998 |
| Popis: | 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 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. |
| Databáze: | OpenAIRE |
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