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The binding of Tritrichomonas foetus to immobilized laminin-1 and its role in the cytotoxicity exerted by the parasite.
- Source :
-
Microbiology (Reading, England) [Microbiology (Reading)] 2008 Aug; Vol. 154 (Pt 8), pp. 2283-2290. - Publication Year :
- 2008
-
Abstract
- The recognition and binding of pathogens to extracellular matrix glycoproteins may determine the outcome of infective processes. The interaction between the bovine urogenital parasite Tritrichomonas foetus and the major basal membrane glycoprotein laminin-1 (LMN-1) was investigated. The chemical nature of parasite molecules involved in the attachment of T. foetus to immobilized LMN-1 and the influence of LMN-1 in the toxicity exerted by the parasite to HeLa cells was studied. Attachment of T. foetus to LMN-1 resulted in notable morphological alterations of the parasite, which became amoeboid. T. foetus recognized LMN-1 through specific amino acid sequences (AG73, C16, A208 and A13) in the LMN-1 molecule, and the protein nature of the parasite molecules involved in the recognition was demonstrated by dot-blot analyses. Such molecular recognition was cation-dependent and five LMN-1-binding molecules (220, 200, 130, 125 and 80 kDa) were identified in T. foetus. Binding of T. foetus to LMN-1 rendered the parasite toxic to HeLa cell monolayers. Thus, LMN-1 appears to provide signalling cues that mediate important cell functions in T. foetus concerning its interaction with host cells.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
Cattle Diseases metabolism
Cell Adhesion
HeLa Cells
Host-Parasite Interactions
Humans
Laminin chemistry
Laminin genetics
Male
Protein Binding
Protozoan Infections metabolism
Protozoan Infections parasitology
Protozoan Proteins chemistry
Protozoan Proteins genetics
Protozoan Proteins metabolism
Tritrichomonas foetus genetics
Tritrichomonas foetus pathogenicity
Cattle Diseases parasitology
Laminin metabolism
Protozoan Infections, Animal
Tritrichomonas foetus metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1350-0872
- Volume :
- 154
- Issue :
- Pt 8
- Database :
- MEDLINE
- Journal :
- Microbiology (Reading, England)
- Publication Type :
- Academic Journal
- Accession number :
- 18667561
- Full Text :
- https://doi.org/10.1099/mic.0.2007/015941-0