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dc.contributor.authorSoares, Regina MA
dc.contributor.authorSilva-Filho, Fernando Costa
dc.contributor.authorRozental, Sonia
dc.contributor.authorAngluster, Jayme
dc.contributor.authorSouza, Wanderley de
dc.contributor.authorAlviano, Celuta Sales
dc.contributor.authorTravassos, Luiz Rodolpho [UNIFESP]
dc.date.accessioned2018-06-18T11:04:05Z
dc.date.available2018-06-18T11:04:05Z
dc.date.issued1998-02-01
dc.identifierhttp://dx.doi.org/10.1099/00221287-144-2-309
dc.identifier.citationMicrobiology-uk. Reading: Soc General Microbiology, v. 144, n. 2, p. 309-314, 1998.
dc.identifier.issn1350-0872
dc.identifier.urihttp://repositorio.unifesp.br/11600/44906
dc.description.abstractThe surface anionogenic groups and sialoglycoconjugate structures of Paracoccidioides brasiliensis yeast forms were analysed by cell microelectrophoresis, binding assays with lectins and viral particles, ultrastructural cytochemistry, enzymic digestion and flow cytofluorimetry. P. brasiliensis yeast forms, particularly the budding primordia, reacted strongly with cationized ferritin. Binding assays showed that the reaction with sialic-acid-specific Limax flavus lectin (LFA) was distributed over the entire P. brasiliensis cell wall. Treatment of yeast forms with neuraminidase significantly reduced their negative surface charge and LFA labelling, which suggests that sialic acid residues are major anionogenic groups exposed on the P. brasiliensis surface. Furthermore, after neuraminidase treatment, labelling with Arachis hypogaea (peanut) agglutinin increased due to unmasking of subterminal beta-D-galactopyranosyl residues. The sialic acid linkages to galactose are alpha 2,6 and alpha 2,3 as assessed, respectively, by fungal attachment to M1/5 and M1/5 HS8 strains of influenza A virus and binding of Sambucus niger and Maackia amurensis agglutinins. The alpha 2,6 linkage clearly predominated in both experiments. Flow cytofluorimetry analysis revealed the heterogenicity of P. brasiliensis yeast cell populations, which comprised young and mature budding yeasts. Both express binding sites to LFA and Limulus polyphemus agglutinin.en
dc.format.extent309-314
dc.language.isoeng
dc.publisherSoc General Microbiology
dc.relation.ispartofMicrobiology-uk
dc.rightsAcesso aberto
dc.subjectanionogenic groupsen
dc.subjectinfluenza virusen
dc.subjectParacoccidioides brasiliensisen
dc.subjectsialic acidsen
dc.subjectyeast formsen
dc.titleAnionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensisen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUniv Estadual Norte Fluminense
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUFRJ, Inst Microbiol Prof Paulo de Goes, Ilha Fundao, BR-21941590 Rio De Janeiro, Brazil
dc.description.affiliationUFRJ, Inst Biofis Carlos Chagas Filho, Ilha Fundao, BR-21949970 Rio De Janeiro, Brazil
dc.description.affiliationUniv Estadual Norte Fluminense, Ctr Biociecias & Biotecnol, BR-28015620 Campos, RJ, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, Brazil
dc.identifier.doi10.1099/00221287-144-2-309
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000071989700009


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