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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 212817, 8 pages
http://dx.doi.org/10.1155/2010/212817
Research Article

Excreted/Secreted Proteins from Trypanosome Procyclic Strains

1UMR 177, IRD-CIRAD, CIRAD TA A-17 / G, Campus International de Baillarguet, 34398 Montpellier Cedex 5, France
2UMR, CNRS 5554, Institut des Sciences de l'Evolution, Université Montpellier II, 34095 Montpellier Cedex 5, France
3Organisation des Nations Unies, INRA, UR1199, LPF; 2 place Pierre Viala Bât., 13 34060 Montpellier Cedex 01, France
4UFR Odontologie, EA 4203, 545 Avenue du Pr Viala, Université Montpellier I, 34193 Montpellier Cedex 5, France

Received 22 July 2009; Accepted 19 September 2009

Academic Editor: Luis I. Terrazas

Copyright © 2010 Celestine Michelle Atyame Nten et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. P. Barrett, “The rise and fall of sleeping sickness,” The Lancet, vol. 367, no. 9520, pp. 1377–1378, 2006. View at Publisher · View at Google Scholar · View at PubMed
  2. WHO, “Human African trypanosomiasis (sleeping sickness): epidemiological update,” The Weekly Epidemiological Record, vol. 81, no. 8, pp. 71–80, 2006.
  3. E. Reinhardt, “Travailler ensemble : la mouche tsé-tsé et la pauvreté rurale,” Chronique ONU, ONU Editor, September 2002, http://www.un.org/french/pubs/chronique/2002/numero2/0202p17_la_mouche_tsetse.html.
  4. E. Matovu, T. Seebeck, J. C. K. Enyaru, and R. Kaminsky, “Drug resistance in Trypanosoma brucei spp., the causative agents of sleeping sickness in man and nagana in cattle,” Microbes and Infection, vol. 3, no. 9, pp. 763–770, 2001. View at Publisher · View at Google Scholar
  5. R. V. M. Rio, Y. Hu, and S. Aksoy, “Strategies of the home-team: symbioses exploited for vector-borne disease control,” Trends in Microbiology, vol. 12, no. 7, pp. 325–336, 2004. View at Publisher · View at Google Scholar · View at PubMed
  6. C. Dale, S. C. Welburn, I. Maudlin, and P. J. M. Milligan, “The kinetics of maturation of trypanosome infections in tsetse,” Parasitology, vol. 111, no. 2, pp. 187–191, 1995.
  7. P. J. M. Milligan, I. Maudlin, and S. C. Welburn, “Trypanozoon: infectivity to humans is linked to reduced transmissibility in tsetse. II. Genetic mechanisms,” Experimental Parasitology, vol. 81, no. 3, pp. 409–415, 1995. View at Publisher · View at Google Scholar · View at PubMed
  8. S. C. Welburn, I. Maudlin, and P. J. M. Milligan, “Trypanozoon: infectivity to humans is linked to reduced transmissibility in tsetse. I. Comparison of human serum-resistant and human serum-sensitive field isolates,” Experimental Parasitology, vol. 81, no. 3, pp. 404–408, 1995. View at Publisher · View at Google Scholar · View at PubMed
  9. I. Maudlin and S. C. Welburn, “Lectin mediated establishment of midgut infections of Trypanosoma congolense and Trypanosoma brucei in Glossina morsitans,” Tropical Medicine and Parasitology, vol. 38, no. 3, pp. 167–170, 1987.
  10. I. Maudlin and S. C. Welburn, “The role of lectins and trypanosome genotype in the maturation of midgut infections in Glossina morsitans,” Tropical Medicine and Parasitology, vol. 39, no. 1, pp. 56–58, 1988.
  11. C. Hu and S. Aksoy, “Innate immune responses regulate trypanosome parasite infection of the tsetse fly Glossina morsitans morsitans,” Molecular Microbiology, vol. 60, no. 5, pp. 1194–1204, 2006. View at Publisher · View at Google Scholar · View at PubMed
  12. E. T. MacLeod, I. Maudlin, A. C. Darby, and S. C. Welburn, “Antioxidants promote establishment of trypanosome infections in tsetse,” Parasitology, vol. 134, no. 6, pp. 827–831, 2007. View at Publisher · View at Google Scholar · View at PubMed
  13. E. T. Macleod, A. C. Darby, I. Maudlin, and S. C. Welburn, “Factors affecting trypanosome maturation in tsetse flies,” PLoS ONE, vol. 2, no. 2, article e239, 2007. View at Publisher · View at Google Scholar · View at PubMed
  14. S. K. Moloo and S. B. Kutuza, “Comparative study on the infection rates of different laboratory strains of Glossina species by Trypanosoma congolense,” Medical and Veterinary Entomology, vol. 2, no. 3, pp. 253–257, 1988.
  15. S. K. Moloo and S. B. Kutuza, “Comparative study on the susceptibility of different Glossina species to Trypanosoma brucei brucei infection,” Tropical Medicine and Parasitology, vol. 39, no. 3, pp. 211–213, 1988.
  16. I. Maudlin, “Inheritance of susceptibility to Trypanosoma congolense infection in Glossina morsitans,” Annals of Tropical Medicine and Parasitology, vol. 76, no. 2, pp. 225–227, 1982.
  17. S. Ravel, D. Patrel, M. Koffi, V. Jamonneau, and G. Cuny, “Cyclical transmission of Trypanosoma brucei gambiense in Glossina palpalis gambiensis displays great differences among field isolates,” Acta Tropica, vol. 100, no. 1-2, pp. 151–155, 2006. View at Publisher · View at Google Scholar · View at PubMed
  18. W. C. Gibson, T. F. de C Marshall, and D. G. Godfrey, “Numerical analysis of enzyme polymorphismml: a new approach to the epidemiology and taxonomy of trypanosomes of the subgenus Trypanozoon,” Advances in Parasitology, vol. 18, pp. 175–246, 1980.
  19. F. Mathieu-Daude, A. Bicart-See, M.-F. Bosseno, S.-F. Breniere, and M. Tibayrenc, “Identification of Trypanosoma brucei gambiense group I by a specific kinetoplast DNA probe,” The American Journal of Tropical Medicine and Hygiene, vol. 50, no. 1, pp. 13–19, 1994.
  20. D. G. Godfrey, C. M. Scott, W. C. Gibson, D. Mehlitz, and U. Zillmann, “Enzyme polymorphism and the identity of Trypanosoma brucei gambiense,” Parasitology, vol. 94, no. 2, pp. 337–347, 1987.
  21. P. Holzmuller, D. G. Biron, P. Courtois, et al., “Virulence and pathogenicity patterns of Trypanosoma brucei gambiense field isolates in experimentally infected mouse: differences in host immune response modulation by secretome and proteomics,” Microbes and Infection, vol. 10, no. 1, pp. 79–86, 2008. View at Publisher · View at Google Scholar · View at PubMed
  22. H. Schägger and G. Von Jagow, “Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa,” Analytical Biochemistry, vol. 166, no. 2, pp. 368–379, 1987.
  23. J. E. Elias, W. Haas, B. K. Faherty, and S. P. Gygi, “Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations,” Nature Methods, vol. 2, no. 9, pp. 667–675, 2005. View at Publisher · View at Google Scholar · View at PubMed
  24. M. J. Lehane, “Peritrophic matrix structure and function,” Annual Review of Entomology, vol. 42, pp. 525–550, 1997. View at Publisher · View at Google Scholar · View at PubMed
  25. Y. Hu and S. Aksoy, “An antimicrobial peptide with trypanocidal activity characterized from Glossina morsitans morsitans,” Insect Biochemistry and Molecular Biology, vol. 35, no. 2, pp. 105–115, 2005. View at Publisher · View at Google Scholar · View at PubMed
  26. Z. Hao, I. Kasumba, and S. Aksoy, “Proventriculus (cardia) plays a crucial role in immunity in tsetse fly (Diptera: Glossinidiae),” Insect Biochemistry and Molecular Biology, vol. 33, no. 11, pp. 1155–1164, 2003. View at Publisher · View at Google Scholar
  27. Z. Hao, I. Kasumba, M. J. Lehane, W. C. Gibson, J. Kwon, and S. Aksoy, “Tsetse immune responses and trypanosome transmission: implications for the development of tsetse-based strategies to reduce trypanosomiasis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 22, pp. 12648–12653, 2001. View at Publisher · View at Google Scholar · View at PubMed
  28. A. Acosta-Serrano, E. Vassella, M. Liniger, et al., “The surface coat of procyclic Trypanosoma brucei: programmed expression and proteolytic cleavage of procyclin in the tsetse fly,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 4, pp. 1513–1518, 2001. View at Publisher · View at Google Scholar · View at PubMed
  29. M. Liniger, A. Acosta-Serrano, J. Van Den Abbeele, et al., “Cleavage of trypanosome surface glycoproteins by alkaline trypsin-like enzyme(s) in the midgut of Glossina morsitans,” International Journal for Parasitology, vol. 33, no. 12, pp. 1319–1328, 2003. View at Publisher · View at Google Scholar
  30. P. Dukes, A. Kaukas, K. M. Hudson, T. Asonganyi, and J. K. Gashumba, “A new method for isolating Trypanosoma brucei gambiense from sleeping sickness patients,” Transactions of the Royal Society of Tropical Medicine and Hygiene, vol. 83, no. 5, pp. 636–639, 1989.
  31. J. M. Harley and A. J. Wilson, “Comparison between Glossina morsitans, G. pallidipes and G. fuscipes as vectors of trypanosomes of the Trypanosoma congolense group: the proportions infected experimentally and the numbers of infective organisms extruded during feeding,” Annals of Tropical Medicine and Parasitology, vol. 62, no. 2, pp. 178–187, 1968.
  32. J. M. Kazadi, Interactions between vector and trypanosome in determining the vectorial competence of tsetse flies, Ph.D. dissertation, University of Liège, Liège, Belgium, 2000.
  33. J. M. Reifenberg, D. Cuisance, J. L. Frezil, G. Cuny, and G. Duvallet, “Comparison of the susceptibility of different Glossina species to simple and mixed infections with Trypanosoma (Nannomonas) congolense savannah and riverine forest types,” Medical and Veterinary Entomology, vol. 11, no. 3, pp. 246–252, 1997.
  34. D. Richner, R. Brun, and L. Jenni, “Production of metacyclic forms by cyclical transmission of West African Trypanosoma (T.) brucei isolates from man and animals,” Acta Tropica, vol. 45, no. 4, pp. 309–319, 1988.
  35. J. H. McKerrow, E. Sun, P. J. Rosenthal, and J. Bouvier, “The proteases and pathogenicity of parasitic protozoa,” Annual Review of Microbiology, vol. 47, pp. 821–853, 1993.
  36. O. D. Rotstein, “Role of fibrin deposition in the pathogenesis of intraabdominal infection,” European Journal of Clinical Microbiology & Infectious Diseases, vol. 11, no. 11, pp. 1064–1068, 1992. View at Publisher · View at Google Scholar
  37. V. Isakova and P. B. Armstrong, “Imprisonment in a death-row cell: the fates of microbes entrapped in the Limulus blood clot,” The Biological Bulletin, vol. 205, no. 2, pp. 203–204, 2003.
  38. H. K. Kuramitsu, “Proteases of Porphyromonas gingivalis: what don't they do?” Oral Microbiology and Immunology, vol. 13, no. 5, pp. 263–270, 1998. View at Publisher · View at Google Scholar
  39. J. Alexander, G. H. Coombs, and J. C. Mottram, “Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a Th1 response,” The Journal of Immunology, vol. 161, no. 12, pp. 6794–6801, 1998.
  40. S. Reed, J. Bouvier, A. S. Pollack, et al., “Cloning of a virulence factor of Entamoeba histolytica. Pathogenic strains possess a unique cysteine proteinase gene,” The Journal of Clinical Investigation, vol. 91, no. 4, pp. 1532–1540, 1993. View at Publisher · View at Google Scholar · View at PubMed
  41. C. B. Breton, T. Blisnick, H. Jouin, et al., “Plasmodium chabaudi p68 serine protease activity required for merozoite entry into mouse erythrocytes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 20, pp. 9647–9651, 1992. View at Publisher · View at Google Scholar
  42. X. Zang, A. K. Atmadja, P. Gray, et al., “The serpin secreted by Brugia malayi microfilariae, Bm-SPN-2, elicits strong, but short-lived, immune responses in mice and humans,” The Journal of Immunology, vol. 165, no. 9, pp. 5161–5169, 2000.
  43. S. Kettle, A. Alcamí, A. Khanna, R. Ehret, C. Jassoy, and G. L. Smith, “Vaccinia virus serpin B13R(SPI-2) inhibits interleukin-1β-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1β-induced fever,” Journal of General Virology, vol. 78, no. 3, pp. 677–685, 1997.
  44. B. Manoury, W. F. Gregory, R. M. Maizels, and C. Watts, “Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing,” Current Biology, vol. 11, no. 6, pp. 447–451, 2001. View at Publisher · View at Google Scholar
  45. G. Niemirowicz, F. Parussini, F. Agüero, and J. J. Cazzulo, “Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes,” Biochemical Journal, vol. 401, no. 2, pp. 399–410, 2007. View at Publisher · View at Google Scholar · View at PubMed
  46. L. A. Rokeach, P. A. Zimmerman, and T. R. Unnasch, “Epitopes of the Onchocerca volvulus RAL1 antigen, a member of the calreticulin family of proteins, recognized by sera from patients with onchocerciasis,” Infection and Immunity, vol. 62, no. 9, pp. 3696–3704, 1994.
  47. M. Dupuis, E. Schaerer, K.-H. Krause, and J. Tschopp, “The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes,” Journal of Experimental Medicine, vol. 177, no. 1, pp. 1–7, 1993. View at Publisher · View at Google Scholar
  48. D. Nandan, T. Yi, M. Lopez, C. Lai, and N. E. Reiner, “Leishmania EF-1α activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation,” Journal of Biological Chemistry, vol. 277, no. 51, pp. 50190–50197, 2002. View at Publisher · View at Google Scholar · View at PubMed
  49. E. Bursell, “Aspects of the metabolism of amino acids in the tsetse fly, Glossina (Diptera),” Journal of Insect Physiology, vol. 9, no. 4, pp. 439–452, 1963. View at Publisher · View at Google Scholar
  50. B. H. Ter Kuile, “Adaptation of metabolic enzyme activities of Trypanosoma brucei promastigotes to growth rate and carbon regimen,” Journal of Bacteriology, vol. 179, no. 15, pp. 4699–4705, 1997.
  51. M. F. Oliveira, B. L. Timm, E. A. Machado, et al., “On the pro-oxidant effects of haemozoin,” FEBS Letters, vol. 512, no. 1–3, pp. 139–144, 2002. View at Publisher · View at Google Scholar
  52. M. E. Villagrán, C. Marín, I. Rodríguez-Gonzalez, J. A. De Diego, and M. Sánchez-Moreno, “Use of an iron superoxide dismutase excreted by Trypanosoma cruzi in the diagnosis of chagas disease: seroprevalence in rural zones of the state of Queretaro, Mexico,” The American Journal of Tropical Medicine and Hygiene, vol. 73, no. 3, pp. 510–516, 2005.
  53. M. Kabiri and D. Steverding, “Identification of a developmentally regulated iron superoxide dismutase of Trypanosoma brucei,” Biochemical Journal, vol. 360, no. 1, pp. 173–177, 2001. View at Publisher · View at Google Scholar
  54. S. Batra, R. K. Chatterjee, and V. M. L. Srivastava, “Antioxidant enzymes in Acanthocheilonema viteae and effect of antifilarial agents,” Biochemical Pharmacology, vol. 40, no. 10, pp. 2363–2369, 1990. View at Publisher · View at Google Scholar
  55. L. Tang, X. Ou, K. Henkle-Dührsen, and M. E. Selkirk, “Extracellular and cytoplasmic CuZn superoxide dismutases from Brugia lymphatic filarial nematode parasites,” Infection and Immunity, vol. 62, no. 3, pp. 961–967, 1994.
  56. C. Olver and M. Vidal, “Proteomic analysis of secreted exosomes,” Sub-Cellular Biochemistry, vol. 43, pp. 99–131, 2007.
  57. N. Amzallag, B. J. Passer, D. Allanic, et al., “TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway,” Journal of Biological Chemistry, vol. 279, no. 44, pp. 46104–46112, 2004. View at Publisher · View at Google Scholar · View at PubMed
  58. A. Lespagnol, D. Duflaut, C. Beekman, et al., “Exosome secretion, including the DNA damage-induced p53-dependent secretory pathway, is severely compromised in TSAP6/Steap3-null mice,” Cell Death & Differentiation, vol. 15, no. 11, pp. 1723–1733, 2008. View at Publisher · View at Google Scholar · View at PubMed
  59. A. Jones, A. Faldas, A. Foucher, et al., “Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei,” Proteomics, vol. 6, no. 1, pp. 259–267, 2006. View at Publisher · View at Google Scholar · View at PubMed