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Identification and isolation of Trypanosoma cruzi trypomastigote collagen-binding proteins: possible role in cell-parasite interaction

Published online by Cambridge University Press:  06 April 2009

P. Velge ,
M. A. Ouaissi ,
J. Cornette ,
D. Afchain  and
A. Capron
P. Velge
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167-CNRS 624, Institut Pasteur, 1, rue du Professeur A. Calmette, 59019-Lille Cédex, France
M. A. Ouaissi*
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167-CNRS 624, Institut Pasteur, 1, rue du Professeur A. Calmette, 59019-Lille Cédex, France
J. Cornette
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167-CNRS 624, Institut Pasteur, 1, rue du Professeur A. Calmette, 59019-Lille Cédex, France
D. Afchain
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167-CNRS 624, Institut Pasteur, 1, rue du Professeur A. Calmette, 59019-Lille Cédex, France
A. Capron
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167-CNRS 624, Institut Pasteur, 1, rue du Professeur A. Calmette, 59019-Lille Cédex, France
*
*Reprint requests to Dr M. A. Ouaissi.
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Summary

We have shown here that collagen type I bound efficiently to the trypomastigote surface. In addition, monoclonal and polyclonal antibodies against collagen types I and III inhibited the infection of fibroblasts by the parasite. These results suggested the presence of collagen-binding protein(s) on the parasite surface. This protein was identified from trypomastigote surface antigens using affinity chromatography on a Gelatin Ultrogel column (denatured form of collagen). These collagen-binding proteins were revealed as a low-affinity gelatin binding protein (LAG Bp) of 98 kDa, and a high-affinity binding protein (HAG Bp) of 58 and 68 kDa under non-reducing and reducing conditions respectively. In addition, HAG Bp and LAG Bp bound to collagen type I. The 58/68 kDa protein was purified to homogeneity on a wheat germ agglutinin Sepharose column. A polyclonal antibody to this glycoprotein, as well as a monoclonal antibody (McAb) 155D3 produced against the HAG Bp, immunoprecipitated two parasite surface antigens of 160 and 58 kDa under non-reducing conditions which migrated at a position of 80–85 and 68 kDa when reduced. However, only the 80–85 kDa component could be precipitated from [S] methionine-labelled trypomastigote antigens under reducing conditions. The antibodies to the 58/68 kDa glycoprotein as well as McAb 155D3 diminished the invasion of fibroblasts by parasites. Taken together these results suggest that the same receptor binds fibronectin and/or collagen and that both the 80–85 and 58/68 kDa glycoproteins form part of the same receptor. These trypomastigote surface molecules may interact with the host cell fibronectin and/or collagen during the initial phase of parasite-cell recognition.

Type
Research Article
Information
Parasitology , Volume 97 , Issue 2 , October 1988 , pp. 255 - 268
Copyright
Copyright © Cambridge University Press 1988

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References

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