Passive transfer of a monoclonal antibody specific for a sialic acid-dependent epitope on the surface of Trypanosoma cruzi trypomastigotes reduces infection in mice

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dc.contributor.authorFranchin, Giovanni [UNIFESP]
dc.contributor.authorPereira-Chioccola, Vera Lucia [UNIFESP]
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.contributor.authorRodrigues, Mauricio Martins [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionINST DANTE PAZZANESE CARDIOL ESTADO SAO PAULO
dc.date.accessioned2018-06-15T17:38:38Z
dc.date.available2018-06-15T17:38:38Z
dc.date.issued1997-07-01
dc.description.abstractTrypanosoma cruzi, the parasite that causes Chagas' disease, proliferates in the cytosol of mammalian cells. When the trypomastigote forms exit the infected cell, they become extensively sialylated because the parasite contains an enzyme called trans-sialidase. This enzyme efficiently catalyzes the transfer of bound sialic acid residues from host glycoconjugates to acceptors containing terminal beta-galactosyl residues on the parasite surface, The sialic acid accepters are developmentally regulated mucin-like glycoproteins that are extremely abundant on the trypomastigote surface. In the present study, we determined whether passive transfer of monoclonal antibodies specific for sialic acid acceptors could reduce the acute infection induced by T. cruzi in a highly susceptible mouse strain. We found that passive transfer to naive mice of an immunoglobulin G1 monoclonal antibody directed to a sialylated epitope of these mucin-like glycoproteins significantly decreased parasitemia and the number of tissue parasites as measured by a DNA probe specific for T. cruzi. Upon challenge with trypomastigotes, mice which received this antibody also had a significant increase in survival. A statistically significant reduction in parasitemia could be accomplished with relatively small doses of immunoglobulin, and Fab fragments alone could not mediate protective immunity. The precise mechanism of parasite elimination is unknown; however; this monoclonal antibody does not lyse trypomastigotes in vitro in the presence of human complement or mouse spleen cells.en
dc.description.affiliationUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT MICROBIOL IMMUNOL & PARASITOL,BR-04023062 SAO PAULO,BRAZIL
dc.description.affiliationINST DANTE PAZZANESE CARDIOL ESTADO SAO PAULO,LAB XENODIAGNOST,BR-04012180 SAO PAULO,BRAZIL
dc.description.affiliationUnifespUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DEPT MICROBIOL IMMUNOL & PARASITOL,BR-04023062 SAO PAULO,BRAZIL
dc.description.sourceWeb of Science
dc.format.extent2548-2554
dc.identifierhttp://iai.asm.org/content/65/7/2548.abstract
dc.identifier.citationInfection And Immunity. Washington: Amer Soc Microbiology, v. 65, n. 7, p. 2548-2554, 1997.
dc.identifier.issn0019-9567
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/43963
dc.identifier.wosWOS:A1997XF63100007
dc.language.isoeng
dc.publisherAmer Soc Microbiology
dc.relation.ispartofInfection And Immunity
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.titlePassive transfer of a monoclonal antibody specific for a sialic acid-dependent epitope on the surface of Trypanosoma cruzi trypomastigotes reduces infection in miceen
dc.typeinfo:eu-repo/semantics/article
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