Author | Kneipp, Lucimar F. | |
Author | Magalhães, Andressa S. | |
Author | Abi-chacra, Érika de Araújo | |
Author | Souza, Lucieri O. P. | |
Author | Alviano, Celuta S. | |
Author | Santos, André L. S. | |
Author | Fernandes, José R. Meyer | |
Access date | 2017-01-24T16:53:46Z | |
Available date | 2017-01-24T16:53:46Z | |
Document date | 2012 | |
Citation | KNEIPP, Lucimar F, et al. Surface phosphatase in Rhinocladiella aquaspersa: biochemical properties and its involvement with adhesion. Medical Micology, v.50, p.570-578, Aug. 2012. | pt_BR |
ISSN | 1369-3786, | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/16920 | |
Language | eng | pt_BR |
Publisher | Oxford University Press | pt_BR |
Rights | restricted access | |
Subject in Portuguese | Interação celular | pt_BR |
Subject in Portuguese | Ecto-fosfatase | pt_BR |
Subject in Portuguese | Rhinocladiella aquaspersa | pt_BR |
Subject in Portuguese | Cromoblastomicose | pt_BR |
Title | Surface phosphatase in Rhinocladiella aquaspersa: biochemical properties and its involvement with adhesion | pt_BR |
Type | Article | |
DOI | 10.3109/13693786.2011.653835 | |
Abstract | Rhinocladiella aquaspersa is an etiologic agent of chromoblastomycosis, a subcutaneous chronic infectious disease. In the present work, we found that the three morphological forms of this fungus (conidia, mycelia and sclerotic bodies) expressed different levels of ecto-phosphatase activity. Our results demonstrated that surface conidial enzyme is an acid phosphatase, inhibited by sodium salts of molybdate, orthovanadate and fluoride and that the inhibition caused by orthovanadate and molybdate was irreversible. The conidial ecto-phosphatase efficiently released phosphate groups from different phosphorylated substrates, causing a higher rate of phosphate removal when p-nitrophenylphosphate was used as substrate. This ecto-enzyme of R. aquaspersa is modulated by Co(2 +) ions and inorganic phosphate (Pi). Accordingly, removal of Pi from the culture medium resulted in a marked (121-fold) increase of ecto-phosphatase activity. Surface phosphatase activity is apparently involved in fungal adhesive properties, since the attachment of R. aquaspersa to epithelial cells was reversed by the pre-treatment of the conidia with orthovanadate, molybdate and anti-phosphatase antibody. Corroborating this finding, conidia with greater ecto-phosphatase activity (grown in Pi-depleted medium) showed higher adherence to epithelial cells than fungi cultivated in the presence of Pi. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Taxonomia ,Bioquímica e Bioprospecção de Fungos Rio de Janeiro, RJ. Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Taxonomia ,Bioquímica e Bioprospecção de Fungos Rio de Janeiro, RJ. Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro.Instituto de Microbiologia Paulo de Góes. Departamento de Microbiologia Geral. Laboratório de Superfície de Microrganismos. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Uniiversidade Federal do Rio de Janeiro. Laboratório de Estudos Integrados em Bioquímica Microbiana. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro.Instituto de Bioquímica Médica. Laboratório de Bioquímica Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Rhinocladiella aquaspersa | pt_BR |
Subject | chromoblastomycosis | pt_BR |
Subject | ecto-phosphatase | pt_BR |
Subject | cellular interaction | pt_BR |
e-ISSN | 1460-2709 | |
Embargo date | 2030-01-01 | |