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Identification of a fibronectin-like molecule on Eimeria tenella

Published online by Cambridge University Press:  06 April 2009

F. Lopez-Bernad ,
E. Del Cacho ,
M. Gallego ,
J. Quilez  and
C. Sanchez-Acedo
F. Lopez-Bernad
Affiliation:
Department of Animal Pathology, Faculty of Veterinary Sciences, University of Zaragoza, 50013-Zaragoza, Spain
E. Del Cacho*
Affiliation:
Department of Animal Pathology, Faculty of Veterinary Sciences, University of Zaragoza, 50013-Zaragoza, Spain
M. Gallego
Affiliation:
Department of Animal Pathology, Faculty of Veterinary Sciences, University of Zaragoza, 50013-Zaragoza, Spain
J. Quilez
Affiliation:
Department of Pathology and Animal Production, Faculty of Veterinary Sciences, 08193-Bellaterra, Barcelona, Spain
C. Sanchez-Acedo
Affiliation:
Department of Animal Pathology, Faculty of Veterinary Sciences, University of Zaragoza, 50013-Zaragoza, Spain
*
* Corresponding author: Parasitologia y Enfermedades Parasitarias, Facultad de Veterinaria, Miguel Servet 177, 50013-Zaragoza, Spain. +34 76 761556. Fax: + 34 76 761612.
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Summary

The attachment of Eimeria tenella to its target cells as an obligatory intracellular pathogen is essential for the development of disease. Previous reports have established that other intracellular protozoa parasites have either fibronectin, an adhesion protein, or fibronectin receptors, both of which are involved in the interaction with the host cells. In this current research, studies have been undertaken to visualize a surface component that may be involved in the attachment of E. tenella to host cells. For this purpose, monoclonal antibodies, both anti-chicken and anti-human fibronectin, and also anti-chicken integrin were used. Our results show a fibronectin-like molecule with an apparent molecular weight of 110 kDa in mature schizonts and microgametes. Staining with serum directed against chicken integrin revealed immunoreactivity within mature schizonts. Both the fibronectin-like molecule and the integrin may play an important role in the parasite stage-cell interaction and the promotion of parasite uptake.

Keywords

fibronectinintegrinadhesion moleculesEimeria tenellachicken
Type
Research Article
Information
Parasitology , Volume 113 , Issue 6 , December 1996 , pp. 505 - 510
Copyright
Copyright © Cambridge University Press 1996

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References

REFERENCES

Beauvais, A., Erickson, C. A., Goins, T., Craig, S. E., Humphries, M. J., Thyeri, J. P. & Dufour, S. (1995). Changes in the fibronectin-specific integrin expression pattern modify the migratory behavior of sarcoma S180 cells in vitro and in the embryonic environment. Journal of Cellular Biology 128, 699–713.CrossRefGoogle ScholarPubMed
Bouvier, J., Etges, R. J. & Bordier, C. (1985). Identification and purification of membrane and soluble forms of major surface protein of Leishmania promastigotes. Journal of Biological Chemistry 260, 15504–15509.CrossRefGoogle ScholarPubMed
Buck, C. A. & Horwitz, A. F. (1987). Cell surface receptors for extracellular matrix molecules. Annual Review of Cell Biology 3, 179–205.CrossRefGoogle ScholarPubMed
Chang, K. P. (1980). Human cutaneous Leishmania in a mouse macrophage line: propagation and isolation of intracellular parasites. Science 209, 1240–1242.CrossRefGoogle Scholar
Corbi, A. L., Kishimoto, T. K., Miller, L. J. & Springer, T. A. (1988). The human leukocyte adhesion glycoprotein Mac-1 (complement receptor type 3, CD11b) alfa-subunit: cloning, primary structure, and relation to the integrins, von Willebrand factor and factor B. Journal of Biological Chemistry 263, 12403–12411.CrossRefGoogle Scholar
Del Cacho, E., Quilez, J., Lopez-Bernad, F., Sanchez-Acedo, C. & Gallego, M. (1996). Identification of a fibronectin-like molecule on the surface of Leishmania amastigotes. Veterinary Parasitology (in the Press).CrossRefGoogle ScholarPubMed
Dustin, M. L., Rothlein, R., Bhan, A. K., Dinarello, C. A. & Springer, T. A. (1986). Induction by interleukin 1 and interferon-γ: tissue distribution, biochemistry, and function of a natural adherence molecule (intercellular adherence molecule-1). Journal of Immunology 137, 245–254.CrossRefGoogle Scholar
Isberg, R. R. (1991). Discrimination between intracellular uptake and surface adhesion of bacterial pathogens. Science 252, 934–938.CrossRefGoogle ScholarPubMed
Isberg, R. R. & Leong, J. M. (1990). Multiple β1, chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell 60, 861–871.CrossRefGoogle Scholar
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227, 680–685.CrossRefGoogle ScholarPubMed
Mosser, D. M. & Edelson, P. J. (1985). The Mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania major promastigotes. Journal of Immunology 136, 2785–2789.CrossRefGoogle Scholar
Ortega-Barria, E. & Pereira, M. E. A. (1991). A novel Trypanosoma cruzi heparin-binding protein promotes fibroblast adhesion and penetration of engineered bacteria and trypanosomes into mammalian cells. Cell 67, 411–421.CrossRefGoogle ScholarPubMed
Ouaissi, M. A. (1988). Role of the RGD sequence in parasite attachment to host cells. Parasitology Today 4, 169–173.CrossRefGoogle ScholarPubMed
Ouaissi, M. A., Cornette, J. & Capron, A. (1985). Trypanosoma cruzi: modulation of parasite-cell interaction by plasma fibronectin. European Journal of Immunology 15, 1096–1101.CrossRefGoogle ScholarPubMed
Pigott, R. & Power, C. (1993). The Adhesion Molecule. Academic Press, London.Google Scholar
Ruoslahti, E., Engvall, E. & Hayman, E. (1981). Fibronectin: Current concepts of its structure and functions. Collagen and Related Research 1, 95–128.CrossRefGoogle ScholarPubMed
Russell, D. G. & Wright, S. D. (1988). Complement receptor type (CR3) binds to an Arg-Gly-Asp-containing region of the major surface glycoprotein, gp63, of Leishmania promastigotes. Journal of Experimental Medicine 168, 279–292.CrossRefGoogle Scholar
Wang, C. C. (1982). Biochemistry and Physiology of coccidia. In The Biology of the Coccidia (ed. Long, P. L.) pp. 168–188. Edward Arnold Publisher, London.Google Scholar