Author | Silva Neto, Benedito Rodrigues da | |
Author | Silva, Julhiany de Fátima da | |
Author | Giannini, Maria José Soares Mendes | |
Author | Lenzi, Henrique Leonel | |
Author | Soares, Célia Maria de Almeida | |
Author | Pereira, Maristela | |
Access date | 2012-01-16T16:59:36Z | |
Available date | 2012-01-16T16:59:36Z | |
Document date | 2009 | |
Citation | SILVA NETO, Benedito Rodrigues da et al. The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesion. BMC Microbiology, v. 9, n. 272, 2009. | pt_BR |
ISSN | 1471-2180 | |
URI | https://www.arca.fiocruz.br/handle/icict/3735 | |
Sponsorship | This study at the Universidade Federal de Goiás was supported by grants
from the Ministério de Ciência e Tecnologia (MCT), Conselho Nacional de
Desenvolvimento Científico e Tecnológico (CNPq), Financiadora de Estudos
e Projetos (FINEP), and by the International Foundation for Science
(IFS), Stockholm, Sweden, through a grant to M.P.. B.R.S.N. was supported
by a fellowship from Coordenação de Aperfeiçoamento de Ensino Superior
(CAPES). | pt_BR |
Language | eng | pt_BR |
Publisher | BioMedCentral | en |
Rights | open access | |
Title | The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin | pt_BR |
Type | Article | |
DOI | 10.1186/1471-2180-9-272 | |
Abstract | Background: The pathogenic fungus Paracoccidioides brasiliensis is the agent of
paracoccidioidomycosis (PCM). This is a pulmonary mycosis acquired by inhalation of fungal
airborne propagules that can disseminate to several organs and tissues leading to a severe form of
the disease. Adhesion and invasion to host cells are essential steps involved in the internalization
and dissemination of pathogens. Inside the host, P. brasiliensis may use the glyoxylate cycle for
intracellular survival.
Results: Here, we provide evidence that the malate synthase of P. brasiliensis (PbMLS) is located on
the fungal cell surface, and is secreted. PbMLS was overexpressed in Escherichia coli, and polyclonal
antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, PbMLS
was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the
P. brasiliensis yeast phase. PbMLSr and its respective polyclonal antibody produced against this
protein inhibited the interaction of P. brasiliensis with in vitro cultured epithelial cells A549.
Conclusion: These observations indicated that cell wall-associated PbMLS could be mediating the
binding of fungal cells to the host, thus contributing to the adhesion of fungus to host tissues and
to the dissemination of infection, behaving as an anchorless adhesin. | pt_BR |
Affilliation | Universidade Federal de Goiás. Instituto de Ciências Biológicas. Departamento de Bioquímica e Biologia Molecular. Laboratório de Biologia Molecular, Goiânia, GO, Brasil | pt_BR |
Affilliation | Universidade Estadual Paulista. Laboratório de Micologia Clínica. Araraquara, SP, Brasil | pt_BR |
Affilliation | Universidade Estadual Paulista. Laboratório de Micologia Clínica. Araraquara, SP, Brasil | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Patologia. Rio de Janeiro, RJ, Brasil | pt_BR |
Affilliation | Universidade Federal de Goiás. Instituto de Ciências Biológicas. Departamento de Bioquímica e Biologia Molecular. Laboratório de Biologia Molecular, Goiânia, GO, Brasil | pt_BR |
Affilliation | Universidade Federal de Goiás. Instituto de Ciências Biológicas. Departamento de Bioquímica e Biologia Molecular. Laboratório de Biologia Molecular, Goiânia, GO, Brasil | pt_BR |
Subject | Paracoccidioides brasiliensis | pt_BR |
Subject | Glyoxylate cycle | pt_BR |
Subject | Malate synthase | pt_BR |
Subject | Anchorless | pt_BR |
Subject | Adhesins | pt_BR |
DeCS | Paracoccidioides brasiliensis | pt_BR |
DeCS | Malato Sintase | pt_BR |
DeCS | Adesão Celular | pt_BR |