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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/7252
Title: 
The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin
Author(s): 
Institution: 
  • Universidade Federal de Goiás (UFG)
  • Universidade Estadual Paulista (UNESP)
  • Fiocruz MS
ISSN: 
1471-2180
Sponsorship: 
  • Ministerio de Ciência e Tecnologia (MCT)
  • Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
  • Financiadora de Estudos e Projetos (FINEP)
  • International Foundation for Science (IFS), Stockholm, Sweden
  • Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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.
Issue Date: 
24-Dec-2009
Citation: 
Bmc Microbiology. London: Biomed Central Ltd., v. 9, p. 12, 2009.
Time Duration: 
12
Publisher: 
Biomed Central Ltd.
Source: 
http://dx.doi.org/10.1186/1471-2180-9-272
URI: 
http://hdl.handle.net/11449/7252
Access Rights: 
Acesso aberto
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/7252
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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