The mucin-like glycoprotein super-family of Trypanosoma cruzi: structure and biological roles

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dc.contributor.author Acosta-Serrano, A.
dc.contributor.author Almeida, I. C.
dc.contributor.author Freitas, L. H.
dc.contributor.author Yoshida, N.
dc.contributor.author Schenkman, S.
dc.date.accessioned 2016-01-24T12:31:22Z
dc.date.available 2016-01-24T12:31:22Z
dc.date.issued 2001-05-01
dc.identifier http://dx.doi.org/10.1016/S0166-6851(01)00245-6
dc.identifier.citation Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 114, n. 2, p. 143-150, 2001.
dc.identifier.issn 0166-6851
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/26542
dc.description.abstract Trypanosoma cruzi expresses at its surface large amounts of mucin-like glycoproteins. the T. cruzi mucins (TcMUC), a group of highly glycosylated GPI-anchored proteins rich in Thr, Ser, and Pro residues, are expressed in high copy numbers in both insect and mammalian stages of the parasite. These molecules are encoded by a multigene family and contain a unique type of glycosylation consisting of several sialylated O-glycans linked to the protein backbone via Nw-acetylglucosamine residues. the TcMUC are important because of their role in host cell invasion and the ability to induce secretion of proinflammatory cytokines and nitric oxide in activated macrophages. the TcMUC are also significant in being the major substrate for the cell surface trans-sialidase. in this review, we summarize the recent knowledge on the molecular structure and function of this family of T. cruzi glycoproteins. (C) 2001 Elsevier Science B.V. All rights reserved. en
dc.format.extent 143-150
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Molecular and Biochemical Parasitology
dc.rights Acesso restrito
dc.subject Trypanosoma cruzi en
dc.subject mucins en
dc.subject sialic acid en
dc.subject trans-sialidase en
dc.subject GPI en
dc.subject glycosylation en
dc.title The mucin-like glycoprotein super-family of Trypanosoma cruzi: structure and biological roles en
dc.type Resenha
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Johns Hopkins Univ
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
dc.description.affiliation Univ São Paulo, ICB2, Dept Parasitol, BR-05508900 São Paulo, Brazil
dc.description.affiliation UNIFESP, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifesp UNIFESP, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.identifier.doi 10.1016/S0166-6851(01)00245-6
dc.description.source Web of Science
dc.identifier.wos WOS:000168924900002



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