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.
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.
Silva-Filho
F C
FC
UFRJ-Instituto de Biofísica Carlos Chagas Filho, CCS-Bloco G, 21949-900, Rio de Janeiro, Brazil. fcsf@biof.ufrj.br
Kasai
S
S
Nomizu
M
M
López
L B
LB
Melo-Braga
M B
MB
Rocha-Azevedo
B
B
Petrópolis
D B
DB
Horbach
I S
IS
D000818:Animals; D002417:Cattle; D002448:Cell Adhesion; D005109:Extracellular Matrix / Q000737:chemistry; D005260:Female; D006801:Humans; D007797:Laminin / Q000378:metabolism*; D008297:Male; D011528:Protozoan Infections / Q000469:parasitology; D016835:Tritrichomonas foetus / Q000472:pathogenicity* / Q000502:physiology*; D014774:Virulence
D007797:Laminin; C121346:laminin 1