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The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells
Author(s) -
Lähteenmäki Kaarina,
Kukkonen Maini,
Korhonen Timo K
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02775-2
Subject(s) - yersinia pestis , bacterial adhesin , proteases , microbiology and biotechnology , escherichia coli , recombinant dna , biology , plasminogen activator , protease , enterobacteriaceae , bacteria , extracellular matrix , virulence , biochemistry , enzyme , gene , endocrinology , genetics
The plasminogen activator Pla of Yersinia pestis belongs to the omptin family of enterobacterial surface proteases and is responsible for the highly efficient invasion of the plague bacterium from the subcutaneous infection site into the circulation. Y. pestis has been reported to invade human epithelial cells. Here, we investigated the role of Pla in bacterial invasion into human endothelial cells. Expression of Pla in recombinant Escherichia coli XL1(pMRK1) enhanced bacterial invasion into ECV304 cells. The invasiveness was not affected by substitution mutation at the residues S99 or D206 that are needed for the proteolytic activity of Pla. Pla‐expressing bacteria adhered to the extracellular matrix of ECV304 cells. Only weak adhesion and poor invasion were seen with the recombinant E. coli XL1(pMRK2), which expresses the omptin homolog from E. coli . The results identify Pla as an invasion protein of Y. pestis and show that the invasive function does not involve the proteolytic activity of Pla.