Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC

FEMS Microbiol Lett. 1999 Jul 15;176(2):495-501. doi: 10.1111/j.1574-6968.1999.tb13703.x.


Salmonella Rck and PagC are closely related virulence-associated proteins. When expressed in non-adherent, non-invasive laboratory Escherichia coli, both proteins localised to the outer membrane. Only Rck conferred adhesion to culture cells, but both proteins induced bacterial binding to the cell monolayer background, to extracellular matrix (ECM) preparations, and to the ECM component laminin. Laminin binding was saturable and competitive, and was reduced by removal of carbohydrate side chains. Pre-incubation with laminin targeted recombinant Rck and PagC bacteria directly to the eukaryotic cell surface, and eliminated background binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cell Membrane / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Extracellular Matrix / metabolism
  • Genes, Bacterial
  • Laminin / metabolism*
  • Membrane Proteins*
  • Protein Binding
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Salmonella / genetics
  • Salmonella / metabolism*


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Laminin
  • Membrane Proteins
  • Recombinant Proteins
  • pagC protein, Salmonella typhimurium