Adhesive properties of the purified plasminogen activator Pla of Yersinia pestis

FEMS Microbiol Lett. 2006 Sep;262(2):158-62. doi: 10.1111/j.1574-6968.2006.00382.x.

Abstract

The beta-barrel outer membrane protease Pla from Yersinia pestis is an important virulence factor in plague and enables initiation of the bubonic plague. Pla is a multifunctional protease whose expression also enhances bacterial adherence to extracellular matrix. It has remained uncertain whether the increase in cellular adhesiveness results from modification of the bacterial surface by Pla, or whether the Pla molecule is an adhesin. Pla was purified as a His6-fusion protein from Escherichia coli and reconstituted with lipopolysaccharide to an enzymatically active form. Purified His6-Pla was coated onto fluorescent micro-particles (FMPs) that expressed plasminogen activity. Pla-coated FMPs also bound to laminin and to reconstituted basement membrane (Matrigel) immobilized on permanox slides, whereas only poor activity was seen with lipopolysaccharide-coated FMPs or bovine serum albumin-coated FMPs. The results show that the Pla molecule has intrinsic adhesive properties and that purified transmembrane proteins coated onto FMPs can be used for functional assays.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Extracellular Matrix / metabolism
  • Microspheres
  • Plasminogen / metabolism
  • Plasminogen Activators / chemistry
  • Plasminogen Activators / isolation & purification
  • Plasminogen Activators / metabolism*
  • Protein Folding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Yersinia pestis / chemistry*
  • Yersinia pestis / physiology*

Substances

  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Plasminogen
  • Pla protease, Yersinia pestis
  • Plasminogen Activators