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Tipo do documento: Artigo
Título: The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin
Autor: Silva Neto, Benedito Rodrigues da
Silva, Julhiany de Fátima da
Giannini, Maria José Soares Mendes
Lenzi, Henrique Leonel
Soares, Célia Maria de Almeida
Pereira, Maristela
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.
País: Gra-bretanha
Unidade acadêmica: Instituto de Ciências Biológicas - ICB (RG)
Citação: SILVA NETO, Benedito Rodrigues da; SILVA, Julhiany de Fátima da; MENDES-GIANNINI, Maria José Soares; LENZI, Henrique Leonel; SOARES, Célia Maria de Almeida; PEREIRA, Maristela. The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin. BMC Microbiology, London, v. 9, p. 272, Dec. 2009.
Tipo de acesso: Acesso Aberto
Identificador do documento: 10.1186/1471-2180-9-272
Identificador do documento: 10.1186/1471-2180-9-272
Data de publicação: Dez-2009
Aparece nas coleções:IPTSP - Artigos publicados em periódicos

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