How laminin-1 can be recognized by the protozoan parasite Tritrichomonas foetus: possible role played by the extracellular matrix glycoprotein in both cytoadhesion and cytotoxicity exerted by the parasite

Parasitol Int. 2002 Sep;51(3):305-7. doi: 10.1016/s1383-5769(02)00018-1.

Abstract

The isoform 1 of the extracellular matrix glycoprotein Laminin is known to be an important ligand for some parasitic protozoa including Trichomonas vaginalis. The bovine parasite Tritrichomonas foetus seems to display a similar recognition process to laminin-1, as some amino acid sequences found in the LNS module of laminin-1 can also be recognized by this parasite. Which of the laminin-1 residing adhesion sequences are recognized by T. foetus, and the role played by such a protein-cell recognition process in both cytoadhesion and cytotoxicity exerted by the parasite are the subjects briefly reviewed and discussed here.

Publication types

  • Review

MeSH terms

  • Animals
  • Cattle
  • Cell Adhesion
  • Extracellular Matrix / chemistry
  • Female
  • Humans
  • Laminin / metabolism*
  • Male
  • Protozoan Infections / parasitology
  • Tritrichomonas foetus / pathogenicity*
  • Tritrichomonas foetus / physiology*
  • Virulence

Substances

  • Laminin
  • laminin 1