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dc.contributor.authorLourenco, E. V.
dc.contributor.authorPereira, Sandra R UNIFESP]
dc.contributor.authorFaça, Vitor Marcel [UNIFESP]
dc.contributor.authorCoelho-Castelo, Arlete Aparecida Martins
dc.contributor.authorMinéo, José R
dc.contributor.authorRoque-Barreira, Maria Cristina
dc.contributor.authorGreene, Lewis Joel [UNIFESP]
dc.contributor.authorPanunto-Castelo, Ademilson
dc.date.accessioned2016-01-24T12:31:25Z
dc.date.available2016-01-24T12:31:25Z
dc.date.issued2001-07-01
dc.identifierhttp://dx.doi.org/10.1093/glycob/11.7.541
dc.identifier.citationGlycobiology. Cary: Oxford Univ Press Inc, v. 11, n. 7, p. 541-547, 2001.
dc.identifier.issn0959-6658
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26585
dc.description.abstractHost cell invasion by Toxoplasma gondii is a multistep process with one of the first steps being the apical release of micronemal proteins that interact with host receptors. We demonstrate here that micronemal protein 1 (MIC1) is a lactose-binding lectin, MIC1 and MIC4 were recovered in the lactose-eluted (Lac(+)) fraction on affinity chromatography on immobilized lactose of the soluble antigen fraction from tachyzoites of the virulent RH strain, MIC1 and MIC4 were both identified by N-terminal microsequencing. MIC4 was also identified by sequencing cDNA clones isolated from an expression library following screening with mouse polyclonal anti-60/70 kDa (Lac(+) proteins) serum. This antiserum localized the Lac(+) proteins on the apical region of T, gondii tachyzoites by confocal microscopy, the Lac(+) fraction induced hemagglutination (mainly type A human erythrocytes), which was inhibited by beta -galactosides (3 mM lactose and 12 mM galactose) but not by up to 100 mM melibiose (alpha -galactoside), fucose, mannose, or glucose or 0.2 mg/ml heparin, the lectin activity of the Lac(+) preparation was attributed to MIC1, because blotted MIC1, but not native MIC4, bound human erythrocyte type A and fetuin, the copurification of MIC1 and MIC4 may have been due to their association, as reported by others. These data suggest that MIC1 may act through its lectin activity during T, gondii infection.en
dc.format.extent541-547
dc.language.isoeng
dc.publisherOxford Univ Press Inc
dc.relation.ispartofGlycobiology
dc.rightsAcesso aberto
dc.subjectToxoplasma gondiien
dc.subjectmicronemeen
dc.subjectMIC 1en
dc.subjectMIC4en
dc.subjectlactose-binding lectinen
dc.titleToxoplasma gondii micronemal protein MIC1 is a lactose-binding lectinen
dc.typeArtigo
dc.rights.licensehttp://www.oxfordjournals.org/access_purchase/self-archiving_policyb.html
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de Uberlândia (UFU)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniv São Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogenicos, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Posgrad Imunol Basica & APlicada, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Ctr Quim Prot, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Fac Med Ribeirao Preto, Dept Obstet & Ginecol, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv Fed Uberlandia, Inst Ciencias Biomed, BR-38400902 Uberlandia, MG, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, SP, Brazil
dc.identifier.doi10.1093/glycob/11.7.541
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000169850400004


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