1887

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 and the major basal membrane glycoprotein laminin-1 (LMN-1) was investigated. The chemical nature of parasite molecules involved in the attachment of to immobilized LMN-1 and the influence of LMN-1 in the toxicity exerted by the parasite to HeLa cells was studied. Attachment of to LMN-1 resulted in notable morphological alterations of the parasite, which became amoeboid. 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 . Binding of 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 concerning its interaction with host cells.

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2008-08-01
2019-11-12
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References

  1. Alderete, J. F. & Garza, G. E. ( 1988; ). Identification and properties of Trichomonas vaginalis proteins involved in cytadherence. Infect Immun 56, 28–33.
    [Google Scholar]
  2. Alderete, J. F., Lehker, M. W. & Arroyo, R. ( 1995; ). The mechanisms and molecules involved in cytoadherence and pathogenesis of Trichomonas vaginalis. Parasitol Today 11, 70–74.[CrossRef]
    [Google Scholar]
  3. Alvarez-Sanchez, M. E., Avila-Gonzalez, L., Becerril-Garcia, C., Fattel-Facenda, L. V., Ortega-Lopez, J. & Arroyo, R. ( 2000; ). A novel cysteine proteinase (CP65) of Trichomonas vaginalis involved in cytotoxicity. Microb Pathog 28, 193–202.[CrossRef]
    [Google Scholar]
  4. Arrighi, R. B. & Hurd, H. ( 2002; ). The role of Plasmodium berghei ookinete proteins in binding to basal lamina components and transformation into oocysts. Int J Parasitol 32, 91–98.[CrossRef]
    [Google Scholar]
  5. Arroyo, R., Gonzalez-Robles, A., Martinez-Palomo, A. & Alderete, J. F. ( 1993; ). Signalling of Trichomonas vaginalis for amoeboid transformation and adhesion synthesis follows cytoadherence. Mol Microbiol 7, 299–309.[CrossRef]
    [Google Scholar]
  6. Bandyopadhyay, K., Karmakar, S., Ghosh, A. & Das, P. K. ( 2001; ). Role of 67 kDa cell surface laminin binding protein of Leishmania donovani in pathogenesis. J Biochem 130, 141–148.[CrossRef]
    [Google Scholar]
  7. Bissell, M. J. & Barcellos-Hoff, M. H. ( 1987; ). The influence of extracellular matrix on gene expression: is structure the message? J Cell Sci Suppl 8, 327–343.
    [Google Scholar]
  8. BonDurant, R. H. ( 1997; ). Pathogenesis, diagnosis, and management of trichomoniasis in cattle. Vet Clin North Am Food Anim Pract 13, 345–361.
    [Google Scholar]
  9. BonDurant, R. H. ( 2005; ). Venereal diseases of cattle: natural history, diagnosis, and the role of vaccines in their control. Vet Clin North Am Food Anim Pract 21, 383–408.[CrossRef]
    [Google Scholar]
  10. Bradford, M. M. ( 1976; ). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248–254.[CrossRef]
    [Google Scholar]
  11. Corbeil, L. B., Hodgson, J. L., Jones, D. W., Corbeil, R. R., Widders, P. R. & Stephens, L. R. ( 1989; ). Adherence of Tritrichomonas foetus to bovine vaginal epithelial cells. Infect Immun 57, 2158–2165.
    [Google Scholar]
  12. Crouch, M. L. & Alderete, J. F. ( 1999; ). Trichomonas vaginalis interaction with fibronectin and laminin. Microbiology 145, 2835–2843.
    [Google Scholar]
  13. Diamond, L. S. ( 1957; ). The establishment of various trichomonads of animals and man in axenic culture. J Parasitol 43, 488–490.
    [Google Scholar]
  14. Ekblom, P., Lonai, P. & Talts, J. F. ( 2003; ). Expression and biological role of laminin-1. Matrix Biol 22, 35–47.[CrossRef]
    [Google Scholar]
  15. Elola, M. T., Chiesa, M. E., Alberti, A. F., Mordoh, J. & Fink, N. E. ( 2005; ). Galectin-1 receptors in different cell types. J Biomed Sci 12, 13–29.[CrossRef]
    [Google Scholar]
  16. Ferreira, E. O., Lobo, A. L., Petrópolis, D. B., Avelar, K. E. S., Ferreira, M. C., Silva-Filho, F. C. & Domingues, R. M. C. P. ( 2006; ). A Bacteroides fragilis surface glycoprotein mediates the interaction between the bacterium and the extracellular matrix component laminin-1. Res Microbiol 157, 960–966.[CrossRef]
    [Google Scholar]
  17. Fujiwara, S., Shinkai, H., Deutzmann, R., Paulsson, M. & Timpl, R. ( 1988; ). Structure and distribution of N-linked oligosaccharide chains on various domains of mouse tumour laminin. Biochem J 252, 453–461.
    [Google Scholar]
  18. Galán, J. E., Pace, J. & Hayman, M. J. ( 1992; ). Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium. Nature 357, 588–589.[CrossRef]
    [Google Scholar]
  19. Ghosh, A., Bandyopadhyay, K., Kole, L. & Das, P. K. ( 1999; ). Isolation of a laminin binding protein from the protozoan parasite Leishmania donovani that may mediate cell adhesion. Biochem J 337, 551–558.[CrossRef]
    [Google Scholar]
  20. Gordon, V. R., Asen, E. K., Vodkin, M. H. & McLaughlin, G. L. ( 1993; ). Acanthamoeba binds to extracellular matrix proteins in vitro. Invest Ophthalmol Vis Sci 34, 658–662.
    [Google Scholar]
  21. Grimbleby, F. H. & Ntailianas, H. A. ( 1961; ). Binding of trichloroacetic acid by protein. Nature 835–836.
    [Google Scholar]
  22. Gu, M., Wang, W., Song, W. K., Cooper, D. N. M. & Kaufman, S. J. ( 1994; ). Selective modulation of the interaction of α7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation. J Cell Sci 107, 175–181.
    [Google Scholar]
  23. Hernandez-Ramirez, V. I., Anaya-Ruiz, M., Rios, A. & Talamas-Rohana, P. ( 2000; ). Tyrosine kinase activity induces by fibronectin through the β1-integrin-like molecule. Exp Parasitol 95, 85–95.[CrossRef]
    [Google Scholar]
  24. Hynes, R. O. ( 2002; ). Integrins: bidirectional, allosteric signaling machines. Cell 110, 673–687.[CrossRef]
    [Google Scholar]
  25. Kronvall, G. & Jonsson, K. ( 1999; ). Receptins: a novel term for an expanding spectrum of natural and engineered microbial proteins with binding properties for mammalian proteins. J Mol Recognit 12, 38–44.[CrossRef]
    [Google Scholar]
  26. Laemmli, U. K. ( 1970; ). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.[CrossRef]
    [Google Scholar]
  27. Lal, K., Noel, C. J., Field, M. C., Goulding, D. & Hirt, R. P. ( 2006; ). Dramatic reorganisation of Trichomonas endomembranes during amoebal transformation: a possible role for G-protein. Mol Biochem Parasitol 148, 99–102.[CrossRef]
    [Google Scholar]
  28. Li, E., Yang, W. G., Zhang, T. & Stanley, S. L., Jr ( 1995; ). Interaction of laminin with Entamoeba histolytica cysteine proteinases and its effects on amebic pathogenesis. Infect Immun 63, 4150–4153.
    [Google Scholar]
  29. Lockwood, B. C., North, M. J. & Coombs, G. H. ( 1984; ). Trichomonas vaginalis, Tritrichomonas foetus, and Trichomitus batrachorum: comparative proteolytic activity. Exp Parasitol 58, 245–253.[CrossRef]
    [Google Scholar]
  30. López, L. B., Braga, M. B., Lopez, J. O., Arroyo, R. & Costa e Silva-Filho, F. ( 2000; ). Strategies by which some pathogenic trichomonads integrate diverse signals in the decision-making process. An Acad Bras Cienc 72, 173–186.[CrossRef]
    [Google Scholar]
  31. Melo-Braga, M. B., Rocha-Azevedo, B. & Silva-Filho, F. C. ( 2003; ). Tritrichomonas foetus: the role played by iron during parasite interaction with epithelial cells. Exp Parasitol 105, 111–120.[CrossRef]
    [Google Scholar]
  32. Mercurio, A. M. ( 1995; ). Laminin receptors: achieving specificity through cooperation. Trends Cell Biol 5, 419–423.[CrossRef]
    [Google Scholar]
  33. Meza, I. ( 2000; ). Extracellular matrix-induced signaling in Entamoeba histolytica: its role in invasiveness. Parasitol Today 16, 23–28.[CrossRef]
    [Google Scholar]
  34. Nelson, C. M. & Bissel, M. J. ( 2006; ). Of extracellular matrix, scaffolds, and signaling: tissue architecture regulates development, homeostasis, and cancer. Annu Rev Cell Dev Biol 22, 287–309.[CrossRef]
    [Google Scholar]
  35. Nomizu, M., Kim, W. H., Yamamura, K., Utani, A., Otaka, S. Y. A., Roller, P. P., Kleinman, H. K. & Yamada, Y. ( 1995; ). Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides. J Biol Chem 270, 20583–20590.[CrossRef]
    [Google Scholar]
  36. Nomizu, M., Kuratomi, Y., Ponce, M. L., Song, S. Y., Miyoshi, K., Otaka, A., Powell, S. K., Hoffman, M. P., Kleinman, H. K. & Yamada, Y. ( 1997; ). Identification of cell binding sequences in mouse laminin γ1 chain by systematic peptide screening. J Biol Chem 272, 32198–32205.[CrossRef]
    [Google Scholar]
  37. Nomizu, M., Kuratomi, Y., Malinda, K. M., Song, S. Y., Miyoshi, K., Otaka, A., Powell, S. K., Hoffman, M. P., Kleinman, H. K. & Yamada, Y. ( 1998; ). Cell binding sequences in mouse laminin α1 chain. J Biol Chem 273, 32491–32499.[CrossRef]
    [Google Scholar]
  38. Parsonson, I. M., Clark, B. L. & Dufty, J. H. ( 1974; ). The pathogenesis of Tritrichomonas foetus infection in the bull. Aust Vet J 50, 421–423.[CrossRef]
    [Google Scholar]
  39. Parsonson, I. M., Clark, B. L. & Dufty, J. H. ( 1976; ). Early pathogenesis and pathology of Tritrichomonas foetus infection in virgin heifers. J Comp Pathol 86, 59–66.[CrossRef]
    [Google Scholar]
  40. Petrin, D., Delgaty, K., Bhatt, R. & Garber, G. ( 1998; ). Clinical and microbiological aspects of Trichomonas vaginalis. Clin Microbiol Rev 11, 300–317.
    [Google Scholar]
  41. Philips, H. I. ( 1973; ). Dye exclusion tests for cell viability. In Tissue Culture, Methods and Applications, pp. 407–408. Edited by P. F. Kruse & M. K. Patterson. New York: Academic Press.
  42. Plow, E. F., Haas, T. A., Zhang, L., Loftus, J. & Smith, J. W. ( 2000; ). Ligand binding to integrins. J Biol Chem 275, 21785–21788.[CrossRef]
    [Google Scholar]
  43. Rao, S. P., Gehlsen, K. R. & Catanzaro, A. ( 1992; ). Identification of a β1 integrin on Mycobacterium aviumMycobacterium intracellulare. Infect Immun 60, 3652–3657.
    [Google Scholar]
  44. Rocha-Azevedo, B., Melo-Braga, M. B. & Silva-Filho, F. C. ( 2005; ). Intra-strain clonal phenotypic variation of Tritrichomonas foetus is related to the cytotoxicity exerted by the parasite to cultured cells. Parasitol Res 95, 106–112.[CrossRef]
    [Google Scholar]
  45. Saarela, S., Wikstro, B. W., Rhen, M. & Korhonen, T. K. ( 1996; ). The GafD protein of the G (F17) fimbrial complex confers adhesiveness of Escherichia coli to laminin. Infect Immun 64, 2857–2860.
    [Google Scholar]
  46. Schwebke, J. R. & Burgess, D. ( 2004; ). Trichomoniasis. Clin Microbiol Rev 17, 794–803.[CrossRef]
    [Google Scholar]
  47. Silva-Filho, F. C., Elias, A. C. & De Souza, W. ( 1986; ). Futher studies on the surface charge of various strains of Trichomonas vaginalis and Tritrichomonas foetus. Cell Biophys 8, 161–176.
    [Google Scholar]
  48. Silva-Filho, F. C., De Souza, W. & Lopes, J. D. ( 1988; ). Presence of laminin-binding proteins in trichomonads and their role in adhesion. Proc Natl Acad Sci U S A 85, 8042–8046.[CrossRef]
    [Google Scholar]
  49. Silva Filho, F. C., Breier-Saraiva, E. M., Tosta, M. X. & De Souza, W. ( 1989; ). Trichomonas vaginalis and Tritrichomonas foetus secrete a neuraminidase into culture medium. Mol Biochem Parasitol 35, 73–78.[CrossRef]
    [Google Scholar]
  50. Silva-Filho, F. C., Kasai, S., Nomizu, M., Lopez, L. B., Melo-Braga, M. B., Rocha-Azevedo, B., Petrópolis, D. B. & Horbach, I. S. ( 2002; ). 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. Parasitol Int 51, 305–307.[CrossRef]
    [Google Scholar]
  51. Singh, B. N., Lucas, J. J., Beach, D. H., Shin, S. T. & Gilbert, R. O. ( 1999; ). Adhesion of Tritrichomonas foetus to bovine vaginal epithelial cells. Infect Immun 67, 3847–3854.
    [Google Scholar]
  52. Towbin, H., Staehelin, T. & Gordon, J. ( 1979; ). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76, 4350–4354.[CrossRef]
    [Google Scholar]
  53. Woo, H. J., Shaw, L. M., Messier, J. M. & Mercurio, A. M. ( 1990; ). The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2). J Biol Chem 265, 7097–7099.
    [Google Scholar]
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