Use este identificador para citar ou linkar para este item: http://repositorio.bc.ufg.br/handle/ri/14968
Tipo do documento: Artigo
Título: Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein
Autor: Chaves, Edilânia Gomes Araújo
Weber, Simone Schneider
Báo, Sonia Nair
Pereira, Luiz Augusto
Bailão, Alexandre Melo
Borges, Clayton Luiz
Soares, Célia Maria de Almeida
Abstract: Background: Despite being important thermal dimorphic fungi causing Paracoccidioidomycosis, the pathogenic mechanisms that underlie the genus Paracoccidioides remain largely unknown. Microbial pathogens express molecules that can interact with human plasminogen, a protein from blood plasma, which presents fibrinolytic activity when activated into plasmin. Additionally, plasmin exhibits the ability of degrading extracellular matrix components, favoring the pathogen spread to deeper tissues. Previous work from our group demonstrated that Paracoccidioides presents enolase, as a protein able to bind and activate plasminogen, increasing the fibrinolytic activity of the pathogen, and the potential for adhesion and invasion of the fungus to host cells. By using proteomic analysis, we aimed to identify other proteins of Paracoccidioides with the ability of binding to plasminogen. Results: In the present study, we employed proteomic analysis of the secretome, in order to identify plasminogen-binding proteins of Paracoccidioides, Pb01. Fifteen proteins were present in the fungal secretome, presenting the ability to bind to plasminogen. Those proteins are probable targets of the fungus interaction with the host; thus, they could contribute to the invasiveness of the fungus. For validation tests, we selected the protein fructose 1,6-bisphosphate aldolase (FBA), described in other pathogens as a plasminogen-binding protein. The protein FBA at the fungus surface and the recombinant FBA (rFBA) bound human plasminogen and promoted its conversion to plasmin, potentially increasing the fibrinolytic capacity of the fungus, as demonstrated in fibrin degradation assays. The addition of rFBA or anti-rFBA antibodies was capable of reducing the interaction between macrophages and Paracoccidioides, possibly by blocking the binding sites for FBA. These data reveal the possible participation of the FBA in the processes of cell adhesion and tissue invasion/ dissemination of Paracoccidioides. Conclusions: These data indicate that Paracoccidioides is a pathogen that has several plasminogen-binding proteins that likely play important roles in pathogen-host interaction. In this context, FBA is a protein that might be involved somehow in the processes of invasion and spread of the fungus during infection.
Palavras-chave: Fructose 1,6-bisphosphate aldolase
Paracoccidioides
Proteome
Secretome
Plasminogen-binding proteins
País: Gra-bretanha
Unidade acadêmica: Instituto de Ciências Biológicas - ICB (RG)
Citação: CHAVES, Edilânia Gomes Araújo et al. Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein. BMC Microbiology, London, v. 15, n. 53, 2015.
Tipo de acesso: Acesso Aberto
Identificador do documento: 10.1186/s12866-015-0393-9
Identificador do documento: 10.1186/s12866-015-0393-9
URI: http://repositorio.bc.ufg.br/handle/ri/14968
Data de publicação: 2015
Aparece nas coleções:IPTSP - Artigos publicados em periódicos

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