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Longitudinal studies of the immune response of Colombian patients infected with Trypanosoma cruzi and T. rangeli

Published online by Cambridge University Press:  06 April 2009

L. Hudson ,
F. Guhl ,
N. de Sanchez ,
D. Bridge ,
C. A. Jaramillo  and
A. Young
L. Hudson
Affiliation:
Department of Immunology, St George's Hospital Medical School, Cranmer Terrace, London SW17 ORE
F. Guhl
Affiliation:
Departmento de Ciencias Biologicas, Universidad de los Andes, Bogota D.E., Colombia
N. de Sanchez
Affiliation:
Departmento de Ciencias Biologicas, Universidad de los Andes, Bogota D.E., Colombia
D. Bridge
Affiliation:
Department of Immunology, St George's Hospital Medical School, Cranmer Terrace, London SW17 ORE
C. A. Jaramillo
Affiliation:
Departmento de Ciencias Biologicas, Universidad de los Andes, Bogota D.E., Colombia
A. Young
Affiliation:
Department of Immunology, St George's Hospital Medical School, Cranmer Terrace, London SW17 ORE
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Summary

Two groups of patients were examined for anti-Trypanosoma cruzi antibodies by immunofluorescence and ELISA (i) inhabitants of the village and surrounding rural area of Tibu, Norte de Santander, Colombia (n = 327) and (ii) employees of the Empresa Colombiana de Petroleos (ECOPETROL, n = 849). The latter group had a lower rate of positive serology (12 as compared to 29%) but the distributions of antibody titres were very similar in the two groups. A total of 119 serum samples (37 village and 82 ECOPETROL, including 25 seronegative controls) were analysed for their ability to immunoprecipitate the 7 major polypeptides of T. cruzi trypomastigotes of Mr > 72 kDa. Although 10 sera from positive patients showed no immunoprecipitation, all of the remaining positive sera contained antibodies which reacted with the 150, 90 and 85 kDa polypeptides. When the T. cruzi immunofluorescence positive, immunoprecipitation negative sera were retested by ELISA using GP90, all were negative thus suggesting that the patients had had a misdiagnosed T. rangeli infection. The new diagnosis was confirmed by immunofluorescence and ELISA with T. rangeli epimastigotes. Longitudinal studies were carried out on 19 patients from the ECOPETROL group for up to 3–5 years. Five seropositive patients showed a change in their anti-trypomastigote immunoprecipitation profiles over this period; one by loss of a previously recognized high molecular weight band and four others by conversion from a negative to a positive immunoprecipitation profile. These latter patients presented initially with uncomplicated T. rangeli infection but then acquired a T. cruzi superinfection. These patients represent the nucleus of a group in which prospective studies will identify the effect of T. rangeli infection on the course of subsequent South American trypanosomiasis and Chagas' disease.

Type
Research Article
Information
Parasitology , Volume 96 , Issue 3 , June 1988 , pp. 449 - 460
Copyright
Copyright © Cambridge University Press 1988

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References

REFERENCE

Afchain, D., LeRay, D., Fruit, J., & Capron, A., (1979). Antigenic makeup of Trypanosoma cruzi culture forms: identification of a specific component. Journal of Parasitology 65, 507–14.CrossRefGoogle ScholarPubMed
Avila, J. L., Rojas, M., Velazquez-Avila, G., & Rieber, M., (1987). Antibodies to laminin in Trypanosoma rangeli-miecteA subjects. Parasitology Research 73, 178–9.Google Scholar
Cabeza Meckert, P., Cazzulo, J. J., Segura, E. L., Estera, M., Ruiz, A., Gelpi, R., & Laguens, R., (1984). Induction of heart alterations by immunization with subcellular fractions of Crithidia fasciculata. Experientia 40, 171–3.Google Scholar
Guhl, F., Hudson, L., Marinkelle, C. J., Jaramillo, C. A., & Bridge, D., (1987). Clinical Trypanosoma rangeli infection as a complication of Chagas' disease. Parasitology 94, 475–84.CrossRefGoogle ScholarPubMed
Gusmao, R. A., Rassi, A., Rezende, J. M., & Neva, F., (1984). Specific and non-specific lymphocyte blastogenic responses in individuals infected with Trypanosoma cruzi. American Journal of Tropical Medicine and Hygiene 33, 827–34.CrossRefGoogle ScholarPubMed
Hudson, L., (1985). Autoimmune phenomena in chronic chagasic cardiopathy. Parasitology Today 1, 6–9.Google Scholar
Hudson, L., & Britten, V., (1985). Immune response to South American trypanosomiasis and its relationship to Chagas' disease. British Medical Bulletin 41, 175–80.CrossRefGoogle ScholarPubMed
Martins, S., Hudson, L., Krettli, A. U., Cancado, J. R., & Brener, Z., (1985). Human and mouse sera recognise the same polypeptide associated with immunological resistance to Trypanosoma cruzi infection. Clinical and Experimental Immunology 61, 343–50.Google ScholarPubMed
Miles, M. A., (1983). The epidemiology of South American trypanosomiasis, biochemical and immunochemical approaches and their relevance to control. Transactions of the Royal Society of Tropical Medicine and Hygiene 11, 5–23.CrossRefGoogle Scholar
Nogueira, N., Unkeless, J., & Cohn, Z., (1982). Specific glycoproteins on the surface of insect and mammalian stages of Trypanosoma cruzi. Proceedings of the National Academy of Sciences, USA 79, 1259–63.CrossRefGoogle ScholarPubMed
Plata, F., Pons, G. F., & Eisen, H., (1984). Antigenic polymorphism of Trypanosoma cruzi: clonal analysis of trypomastigote surface antigens. European Journal of Immunology 14, 392–9.CrossRefGoogle ScholarPubMed
Plessman Camargo, E., Barbieri, C. L., & Jankevicius, J. V., (1982). Possible artifacts in the radioiodination of surface proteins of trypanosomatids. Journal of Immunological Methods 52, 245–53.Google Scholar
Ruiz, A. M., Estera, M., Cabeza Meckert, P., Laguens, R. P., & Segura, E. L., (1985). Protective immunity and pathology induced by innoculation of mice with different subcellular fractions of Trypanosoma cruzi. Acta Tropica 42, 299–309.Google Scholar
Saravia, N. G., Holguin, A. F., Cibulskis, R. E., & D'Alessandro, A., (1987). Divergent isoenzyme profiles of sylvatic and domiciliary Trypanosoma cruzi in the eastern plains, Piedmont and highlands of Colombia. American Journal of Tropical Medicine and Hygiene 36, 59–69.CrossRefGoogle ScholarPubMed
Schechter, M., Luquetti, A. O., Rezende, J. M., Rassi, A., & Miles, M. A., (1985). Further evaluation of lectin affinity purified glycoprotein (GP90) in the enzyme linked immunosorbent assay (ELISA) for diagnosis of Trypanosoma cruzi infection. Transactions of the Royal Society of Tropical Medicine and Hygiene 79, 637–40.CrossRefGoogle ScholarPubMed
Scott, M. T., & Goss-Sampson, M., (1984). Restricted IgG isotype profiles in T. cruzi infected mice and Chagas' disease patients. Clinical and Experimental Immunology 58, 372–9.Google Scholar
Snary, D., (1985). The cell surface of Trypanosoma cruzi. Current Topics in Microbiology and Immunology 117, 75–92.Google ScholarPubMed
Takle, G., (1988). A simple, well-defined culture medium for the growth of Trypanosoma rangeli. Transactions of the Royal Society of Tropical Medicine and Hygiene (in the Press).CrossRefGoogle Scholar
Warren, L. G., (1960). Metabolism of Schizotrypanum cruzi Chagas. I. Effects of culture age and substrate concentration on the respiratory rate. Journal of Parasitology 46, 529–39.CrossRefGoogle Scholar
Wong, R. C. K., Hudson, L., & Hindmarsh, P. J. E., (1986). Immune precipitation and immunoblotting for the detection of Trypanosoma cruzi antigens. Transactions of the Royal Society of Tropical Medicine and Hygiene 80, 275–81.CrossRefGoogle ScholarPubMed
Zingales, B., Abuin, G., Romanha, A. J., Chiari, E., & Colli, W., (1984). Surface antigens of stocks and clones of Trypanosoma cruzi isolated from humans. Acta Tropica 41, 5–16.Google ScholarPubMed