Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis

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dc.contributor.author Soares, Regina MA
dc.contributor.author Silva-Filho, Fernando Costa
dc.contributor.author Rozental, Sonia
dc.contributor.author Angluster, Jayme
dc.contributor.author Souza, Wanderley de
dc.contributor.author Alviano, Celuta Sales
dc.contributor.author Travassos, Luiz Rodolpho [UNIFESP]
dc.date.accessioned 2018-06-18T11:04:05Z
dc.date.available 2018-06-18T11:04:05Z
dc.date.issued 1998-02-01
dc.identifier http://dx.doi.org/10.1099/00221287-144-2-309
dc.identifier.citation Microbiology-uk. Reading: Soc General Microbiology, v. 144, n. 2, p. 309-314, 1998.
dc.identifier.issn 1350-0872
dc.identifier.uri http://repositorio.unifesp.br/11600/44906
dc.description.abstract The 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.extent 309-314
dc.language.iso eng
dc.publisher Soc General Microbiology
dc.relation.ispartof Microbiology-uk
dc.rights Acesso aberto
dc.subject anionogenic groups en
dc.subject influenza virus en
dc.subject Paracoccidioides brasiliensis en
dc.subject sialic acids en
dc.subject yeast forms en
dc.title Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis en
dc.type Artigo
dc.contributor.institution Universidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institution Univ Estadual Norte Fluminense
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation UFRJ, Inst Microbiol Prof Paulo de Goes, Ilha Fundao, BR-21941590 Rio De Janeiro, Brazil
dc.description.affiliation UFRJ, Inst Biofis Carlos Chagas Filho, Ilha Fundao, BR-21949970 Rio De Janeiro, Brazil
dc.description.affiliation Univ Estadual Norte Fluminense, Ctr Biociecias & Biotecnol, BR-28015620 Campos, RJ, Brazil
dc.description.affiliation Univ Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, Brazil
dc.description.affiliationUnifesp Univ Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, Brazil
dc.identifier.doi 10.1099/00221287-144-2-309
dc.description.source Web of Science
dc.identifier.wos WOS:000071989700009



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