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Yersinia pestis Pla Has Multiple Virulence-associated Functions

  • Kaarina Lähteenmäki
  • Maini Kukkonen
  • Silja Jaatinen
  • Marjo Suomalainen
  • Hanna Soranummi
  • Ritva Virkola
  • Hannu LÅng
  • Timo K. Korhonen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 529)

Conclusions

Our work indicates that Y. pestis Pla is a multifunctional surface protein. It is an efficient protease and also an adhesin and an invasin. The Salmonella homolog of Pla, PgtE, also has proteolytic and adhesive properties, whereas E. coli OmpT is only weakly adhesive, and its substrate specificity differs from that of Pla and PgtE. PgtE and OmpT do not mediate bacterial invasion into any of the human epithelial and endothelial cell lines tested. We are currently characterizing the mechanism and relevance of Pla-mediated invasion as well as the structural requirements of the other functions of Pla.

Keywords

Endothelial Cell Line Bacterial Invasion Yersinia Pestis ECV304 Cell Surface Protease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Kluwer Academic Publishers 2004

Authors and Affiliations

  • Kaarina Lähteenmäki
    • 1
  • Maini Kukkonen
    • 1
  • Silja Jaatinen
    • 1
  • Marjo Suomalainen
    • 1
  • Hanna Soranummi
    • 1
  • Ritva Virkola
    • 1
  • Hannu LÅng
    • 1
  • Timo K. Korhonen
    • 1
  1. 1.Division of General Microbiology, Department of BiosciencesUniversity of HelsinkiHelsinkiFinland

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