Novel mechanism that Trypanosoma cruzi uses to adhere to the extracellular matrix mediated by human galectin-3

Binding of Trypanosoma cruzi trypomastigotes to laminin is enhanced by galectin-3, a β-galactoside binding lectin. The galectin-3 enhanced binding of trypanosomes to laminin is inhibited by lactose. Co-immunoprecipitations indicate that galectin-3 binds to the 45, 32 and 30 kDa trypanosome surface p...

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Bibliographic Details
Published in:FEBS letters 2000-03, Vol.470 (3), p.305-308
Main Authors: Moody, Tapria N., Ochieng, Josiah, Villalta, Fernando
Format: Article
Language:English
Subjects:
Adhesion
Animals
Antibodies, Monoclonal - immunology
Antigens, Differentiation - immunology
Antigens, Differentiation - metabolism
Antigens, Differentiation - pharmacology
Blotting, Western
Cell Adhesion - drug effects
Collagen - metabolism
Cross Reactions - immunology
Extracellular matrix
Extracellular Matrix - drug effects
Extracellular Matrix - metabolism
Extracellular Matrix - parasitology
Galectin 3
Human galectin-3
Humans
Lactose - metabolism
Lactose - pharmacology
Laminin
Laminin - metabolism
Molecular Weight
Mucin
Mucins - chemistry
Mucins - immunology
Mucins - metabolism
Precipitin Tests
Protein Binding - drug effects
Trypanosoma cruzi - chemistry
Trypanosoma cruzi - drug effects
Trypanosoma cruzi - metabolism
Trypanosoma cruzi - physiology
Trypanosoma cruzi surface protein
Variant Surface Glycoproteins, Trypanosoma - chemistry
Variant Surface Glycoproteins, Trypanosoma - immunology
Variant Surface Glycoproteins, Trypanosoma - metabolism
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Summary:Binding of Trypanosoma cruzi trypomastigotes to laminin is enhanced by galectin-3, a β-galactoside binding lectin. The galectin-3 enhanced binding of trypanosomes to laminin is inhibited by lactose. Co-immunoprecipitations indicate that galectin-3 binds to the 45, 32 and 30 kDa trypanosome surface proteins. Binding of galectin-3 to the 45, 32 and 30 kDa surface proteins is inhibited by lactose. Polyclonal and a monoclonal antibodies to galectin-3 immunoprecipitated a major 64 kDa trypanosome surface protein. T. cruzi monoclonal antibody to mucin recognized the 45 kDa surface protein. The 45, 32 and 30 kDa surface proteins interact with galectin-3 in order to enhance trypanosome adhesion to laminin.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01347-8