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Circulating trans-sialidase activity and trans-sialidase-inhibiting antibodies inTrypanosoma cruzi-infected mice

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Abstract

Parasite-derived trans-sialidase (TS) activity was demonstrated in the serum and blood ofTrypanosoma cruzi-infected mice. Serum TS activity levels correlated well with parasitemia in BALB/c and Swiss mice during the initial stages of the infection. However, in later stages the TS activity levels decreased despite increasing parasitemia. This coincided with the appearance of circulating TS antibodies. On the other hand, there was always a good correlation between TS activity and parasitemia in athymic nude mice. Sera from mice with high parasitemia and low TS activity inhibited TS activity in vitro. The inhibition was also observed with purified serum IgG, and it was absorbed by staphylococcal protein A, indicating that it was caused by anti-TS IgG antibodies. These antibodies inhibited the enzymatic activity of insolubilized TS, indicating that they act by interfering with the catalytic site rather than by aggregating the enzyme. The presence of inhibitory antibodies, however, did not prevent the progression of parasitemia in BALB/c mice.

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References

  • Affranchino JL, Ibanez CF, Luquetti AO, Rassi A, Reyes MB, Macina RA, Aslund L, Pettersson U, Frasch ACC (1989) Identification of aTrypanosoma cruzi antigen that is shed during the acute phase of Chagas' disease. Mol Biochem Parasitol 34:221–228

    Google Scholar 

  • Cazzulo JJ, Frasch ACC (1992) SAPA/trans-sialidase and cruzipain: two antigens fromTrypanosoma cruzi contain immunodominant but enzymatically inactive domains. FASEB J 6:3259–3264

    Google Scholar 

  • Chaves LB, Briones MRS, Schenkman S (1993) Trans-sialidase fromTrypanosoma cruzi epimastigote is expressed at the stationary phase of growth and is different from the enzyme expressed in trypomastigotes. Mol Biochem Parasitol 61:97–106

    Google Scholar 

  • Frevert U, Schenkman S, Nussenzweig V (1992) Stage-specific expression and intracellular shedding of the cell surface trans-sialidase ofTrypanosoma cruzi. Infect Immun 60:2349–2360

    Google Scholar 

  • Hall BF, Webster P, Ma AK, Joiner KA, Andrews NW (1992) Desialylation of lysosomal membrane glycoproteins byTrypanosoma cruzi: a role for the surface neuraminidase in facilitating parasite entry into the host cell cytoplasm. J Exp Med 176:313–325

    Google Scholar 

  • Hudson L, Hay FC (1980) Practical immunology, Blackwell, Oxford London Edinburgh Boston Melbourne

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Google Scholar 

  • Leguizamon MS, Campetella OE, Gonzalez-Cappa SM, Frasch AC (1994) Mice infected withTrypanosoma cruzi produce antibodies against the enzymatic domain of trans-sialidase that inhibit its activity. Infect Immun 62:3441–3446

    Google Scholar 

  • Libby P, Alroy J, Pereira ME (1986) A neuraminidase fromTrypanosoma cruzi removes sialic acid from the surface of mammalian myocardial and endothelial cells. J Clin Invest 77:127–135

    Google Scholar 

  • Medina-Acosta E, Paul S, Tomlinson S, Pontes de Carvalho LC (1994) Combined occurrence of trypanosomal sialidase/trans-sialidase activities and leishmanial metalloproteinase gene homologoues inEndotrypanum sp. Mol Biochem Parasitol 64:273–282

    Google Scholar 

  • Ming M, Chuenkova M, Ortega-Barria E, Pereira MEA (1993) Mediation ofTrypanosoma cruzi invasion by sialic acid on the host cell and trans-sialidase on the trypanosome. Mol Biochem Parasitol 59:243–252

    Google Scholar 

  • Parodi AJ, Pollevick GD, Mautner M, Buschiazzo A, Sanchez DO, Frasch AC (1992) Identification of the gene(s) coding for the trans-sialidase ofTrypanosoma cruzi. EMBO J 11:1705–1710

    Google Scholar 

  • Pereira ME (1983) A developmentally regulated neuraminidase activity inTrypanosoma cruzi. Science 219:1444–1446

    Google Scholar 

  • Pereira MEA, Mejia JS, Ortega-Barria D, Matzilevich D, Prioli RP (1991) TheTrypanosoma cruzi neuraminidase contains sequences similar to bacterial neuraminidases, YWTD repeats of the low density lipoprotein receptor, and type III modules of fibronectin. J Exp Med 174:179–191

    Google Scholar 

  • Pereira-Chioccola VL, Schenkman S, Kloetzel JK (1994) Sera from chronic chagasic patients and rodends infected withTrypanosoma cruzi inhibit trans-sialidase by recognizing its amino-terminal and catalytic domain. Infect Immun 62:2973–2978

    Google Scholar 

  • Pontes de Carvalho LC, Tomlinson S, Vandekerckhove F, Bienen EJ, Clarkson A, Jiang MS, Hart GW, Nussenzweig V (1993) Characterization of a novel trans-sialidase ofTrypanosoma brucei procyclic trypomastigotes and identification of procyclin as a sialic acid acceptor. J Exp Med 177:465–474

    Google Scholar 

  • Rossi MA, Teixeira ARL, Ribeiro-dos-Santos R (1984) ExperimentalTrypanosoma cruzi cardiomyopathy in BALB/c mice. Am J Pathol 114:209–216

    Google Scholar 

  • Schenkman S, Jiang MS, Hart GW, Nussenzweig V (1991) A novel cell surface trans-sialidase ofTrypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells. Cell 65:1117–1125

    Google Scholar 

  • Schenkman S, Kurosaki T, Ravetch J, Nussenzweig V (1992a) Evidence for the participation of the Ssp-3 antigen in the invasion of non-phagocytic mammalian cells byTrypanosoma cruzi. J Exp Med 175:1635–1641

    Google Scholar 

  • Schenkman S, Pontes de Carvalho L, Nussenzweig V (1992b)Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes. J Exp Med 175:567–575

    Google Scholar 

  • Silva LHP, Nussenzweig V (1953) Sobre uma cepa deTrypanosoma cruzi altamente virulenta para o camundongo branco. Folia Clin Biol 20:191–203

    Google Scholar 

  • Titto EH de, Araujo FG (1988) Serum neuraminidase activity and hematological alterations in acute human Chagas' disease. Clin Immunol Immunopathol 46:157–161

    Google Scholar 

  • Uemura H, Schenkman S, Nussenzweig V, Eichinger D (1992) Only some members of a gene family inTrypanosoma cruzi encode proteins which express both trans-sialidase and neuraminidase activities. EMBO J 11:3837–3844

    Google Scholar 

  • Vandekerckhove F, Schenkman S, Pontes de Carvalho LC, Tomlinson S, Kiso M, Yoshida M, Hasegawa A, Nussenzweig V (1992) Substrate-specificity of theTrypanosoma cruzi trans-sialidase. Glycobiology 2:541–548

    Google Scholar 

  • Voller A, Bartlett A, Bidwell DE (1976) Enzyme immunoassays with special reference to ELISA techniques. J Clin Pathol 31:507–520

    Google Scholar 

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Alcântara-Neves, N.M., Pontes-de-Carvalho, L.C. Circulating trans-sialidase activity and trans-sialidase-inhibiting antibodies inTrypanosoma cruzi-infected mice. Parasitol Res 81, 560–564 (1995). https://doi.org/10.1007/BF00932022

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  • DOI: https://doi.org/10.1007/BF00932022

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