Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/11600/44906 http://dx.doi.org/10.1099/00221287-144-2-309 |
Resumo: | 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. |
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Soares, Regina MASilva-Filho, Fernando CostaRozental, SoniaAngluster, JaymeSouza, Wanderley deAlviano, Celuta SalesTravassos, Luiz Rodolpho [UNIFESP]Universidade Federal do Rio de Janeiro (UFRJ)Univ Estadual Norte FluminenseUniversidade Federal de São Paulo (UNIFESP)2018-06-18T11:04:05Z2018-06-18T11:04:05Z1998-02-01Microbiology-uk. Reading: Soc General Microbiology, v. 144, n. 2, p. 309-314, 1998.1350-0872http://repositorio.unifesp.br/11600/44906http://dx.doi.org/10.1099/00221287-144-2-30910.1099/00221287-144-2-309WOS:000071989700009The 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.UFRJ, Inst Microbiol Prof Paulo de Goes, Ilha Fundao, BR-21941590 Rio De Janeiro, BrazilUFRJ, Inst Biofis Carlos Chagas Filho, Ilha Fundao, BR-21949970 Rio De Janeiro, BrazilUniv Estadual Norte Fluminense, Ctr Biociecias & Biotecnol, BR-28015620 Campos, RJ, BrazilUniv Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, BrazilUniv Fed Sao Paulo, Disciplina Biol Celular, BR-04023062 Sao Paulo, BrazilWeb of Science309-314engSoc General MicrobiologyMicrobiology-ukanionogenic groupsinfluenza virusParacoccidioides brasiliensissialic acidsyeast formsAnionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/449062022-02-08 11:52:12.256metadata only accessoai:repositorio.unifesp.br:11600/44906Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-02-08T14:52:12Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
title |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
spellingShingle |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis Soares, Regina MA anionogenic groups influenza virus Paracoccidioides brasiliensis sialic acids yeast forms |
title_short |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
title_full |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
title_fullStr |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
title_full_unstemmed |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
title_sort |
Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis |
author |
Soares, Regina MA |
author_facet |
Soares, Regina MA Silva-Filho, Fernando Costa Rozental, Sonia Angluster, Jayme Souza, Wanderley de Alviano, Celuta Sales Travassos, Luiz Rodolpho [UNIFESP] |
author_role |
author |
author2 |
Silva-Filho, Fernando Costa Rozental, Sonia Angluster, Jayme Souza, Wanderley de Alviano, Celuta Sales Travassos, Luiz Rodolpho [UNIFESP] |
author2_role |
author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal do Rio de Janeiro (UFRJ) Univ Estadual Norte Fluminense Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Soares, Regina MA Silva-Filho, Fernando Costa Rozental, Sonia Angluster, Jayme Souza, Wanderley de Alviano, Celuta Sales Travassos, Luiz Rodolpho [UNIFESP] |
dc.subject.eng.fl_str_mv |
anionogenic groups influenza virus Paracoccidioides brasiliensis sialic acids yeast forms |
topic |
anionogenic groups influenza virus Paracoccidioides brasiliensis sialic acids yeast forms |
description |
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. |
publishDate |
1998 |
dc.date.issued.fl_str_mv |
1998-02-01 |
dc.date.accessioned.fl_str_mv |
2018-06-18T11:04:05Z |
dc.date.available.fl_str_mv |
2018-06-18T11:04:05Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Microbiology-uk. Reading: Soc General Microbiology, v. 144, n. 2, p. 309-314, 1998. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/11600/44906 http://dx.doi.org/10.1099/00221287-144-2-309 |
dc.identifier.issn.none.fl_str_mv |
1350-0872 |
dc.identifier.doi.none.fl_str_mv |
10.1099/00221287-144-2-309 |
dc.identifier.wos.none.fl_str_mv |
WOS:000071989700009 |
identifier_str_mv |
Microbiology-uk. Reading: Soc General Microbiology, v. 144, n. 2, p. 309-314, 1998. 1350-0872 10.1099/00221287-144-2-309 WOS:000071989700009 |
url |
http://repositorio.unifesp.br/11600/44906 http://dx.doi.org/10.1099/00221287-144-2-309 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Microbiology-uk |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
309-314 |
dc.publisher.none.fl_str_mv |
Soc General Microbiology |
publisher.none.fl_str_mv |
Soc General Microbiology |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1802764156244328448 |