MUCIN-LIKE GLYCOPROTEINS LINKED TO the MEMBRANE BY GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR ARE the MAJOR ACCEPTORS of SIALIC-ACID in A REACTION CATALYZED BY TRANS-SIALIDASE in METACYCLIC FORMS of TRYPANOSOMA-CRUZI

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dc.contributor.authorSchenkman, S.
dc.contributor.authorFerguson, MAJ
dc.contributor.authorHeise, N.
dc.contributor.authorDealmeida, MLC
dc.contributor.authorMortara, R. A.
dc.contributor.authorYoshida, N.
dc.contributor.institutionUNIV DUNDEE
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T11:40:13Z
dc.date.available2016-01-24T11:40:13Z
dc.date.issued1993-06-01
dc.description.abstractWe have previously shown that 35- and 50-kDa glycoconjugates of cultured metacyclic trypomastigotes participate in the attachment of parasites to mammalian cells. Here we show that when metacyclic trypomastigotes are incubated with [H-3]sialyllactose, most of the sialic acid is transferred to these 35/50-kDa molecules in a reaction catalyzed by a parasite transsialidase. the sialic acid is incorporated in oligosaccharides of about 10 glucose units in size that are released from the glycoconjugate by mild alkaline hydrolysis. Compositional analysis reveals that the 35/50-kDa molecules are highly glycosylated proteins rich in threonine, galactose, N-acetyl-glucosamine and sialic acid. These glycoproteins can be labeled in vivo with [H-3]palmitate, and the labeled fatty acid is released by glycosylphosphatidylinositol specific phospholipases C. This result, associated with the fact that they contain mannose, ethanolamine, myo-inositol, and lipid, indicate that these glycoproteins are anchored to the membrane by glycosylphosphatidylinositol. During cell invasion, these molecules appear to be capped and locally released by the parasite.en
dc.description.affiliationUNIV DUNDEE,DEPT BIOCHEM,DUNDEE DD1 4HN,SCOTLAND
dc.description.sourceWeb of Science
dc.format.extent293-303
dc.identifierhttp://dx.doi.org/10.1016/0166-6851(93)90227-O
dc.identifier.citationMolecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 59, n. 2, p. 293-303, 1993.
dc.identifier.doi10.1016/0166-6851(93)90227-O
dc.identifier.issn0166-6851
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/25331
dc.identifier.wosWOS:A1993LE84900012
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular and Biochemical Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTRYPANOSOMA-CRUZIen
dc.subjectSIALIC ACIDen
dc.subjectTRANS-SIALIDASEen
dc.subjectCELL INVASIONen
dc.subjectGLYCOSYLPHOSPHATIDYLINOSITOLen
dc.titleMUCIN-LIKE GLYCOPROTEINS LINKED TO the MEMBRANE BY GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR ARE the MAJOR ACCEPTORS of SIALIC-ACID in A REACTION CATALYZED BY TRANS-SIALIDASE in METACYCLIC FORMS of TRYPANOSOMA-CRUZIen
dc.typeinfo:eu-repo/semantics/article
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