A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics

Rezende, Tereza Cristina Vieira de; Borges, Clayton Luiz; Magalhães, Adriana Dias; Sousa, Marcelo Valle de; Ricart, Carlos André Ornelas; Bailão, Alexandre Mello; Soares, C. M. A.

doi:10.1016/j.jprot.2011.08.020

Cited by 42 publications

(62 citation statements)

References 34 publications

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“…Two-dimensional fractionation (2-DE) of secreted proteins was performed, as described [77,80]. The 2-DE gels were obtained in duplicates, using 500 μg of proteins, for each one.…”

Section: Methodsmentioning

confidence: 99%

Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein

et al. 2015

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BackgroundDespite 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.ResultsIn 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.ConclusionsThese 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.

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“…Two-dimensional fractionation (2-DE) of secreted proteins was performed, as described [77,80]. The 2-DE gels were obtained in duplicates, using 500 μg of proteins, for each one.…”

Section: Methodsmentioning

confidence: 99%

Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein

et al. 2015

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“…The C-H stretching (str) region shows difference in fatty acids for yeast forms in the modes at 2921 cm -1 (str asymmetric of CH 2 ) and 2852cm -1 (str symmetric of CH 2 ) [9]. A hypothesis is that fatty acids might be an important carbon and energy source for P. brasiliensis in the mycelia-toyeast transition and in the yeast itself [4].…”

Section: Comparison Between Ft-ir Spectra Of Yeast and Myceliummentioning

confidence: 99%

“…However, the yeast phase has an energy metabolism, which is based on fermentation process that leads to ethanol production. The glyoxylate pathway is also more active in the yeast form [4,5].…”

Section: Introductionmentioning

confidence: 99%

Biochemical differentiation of mycelium and yeast forms of Paracoccidioides brasiliensis by Fourier transform infrared spectroscopy

et al. 2012

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Paracoccidioides brasiliensis the etiological agent of paracoccidioidomycosis, is a dimorphic fungus existing as mycelia in the environment (or at 25 °C in vitro) and as yeast cells in the human host (or at 37 °C in vitro). The most prominent difference between both forms is probably the cell wall polysaccharide, being 1,3-ß-glucan usually found in mycelia and 1,3-α-glucan found in yeasts, but a plethora of other differences have already been described. In this work, we performed a Fourier Transform Infrared Spectroscopy analysis to compare the yeast and mycelia forms of P. brasiliensis and found additional biochemical differences. The analysis of the spectra showed that differences were distributed in chemical bonds of proteins, lipids and carbohydrates.

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“…Análises transcricionais e proteômicas têm ajudado na compreensão do dimorfismo de (Rezende et al, 2011).…”

Section: Pb18) Foram Finalizados Por Meio Do Projeto Denominado "Genôunclassified

“…Análises proteômicas realizada por Winters e colaboradores (2008) (2011) demonstraram que na transição de micélio para levedura ocorre aumento na expressão das enzimas álcool desidrogenase, fosfoglicomutase e enolase. Assim como enzimas da via das pentoses fosfato, como transcetolase e transaldolase, sugerindo que a indução da via durante a transição poderia fornecer substratos para as enzimas da glicólise, que se mostrou induzida na forma de levedura (Rezende et al, 2011). O aumento de expressão da enzima álcool desidrogenase, após 22 horas de transição, bem como de uma enzima da via do ácido tricarboxílico, a succinil CoA, sugere que tanto a fermentação quanto a respiração aeróbia estão presentes na fase de levedura (Rezende et al, 2011).…”

Section: Análise Proteômica De Fungos Patogênicos Humanosunclassified

Remodelamento metabólico de Paracoccidioides lutzii durante a privação de cobre determinado por análises proteômicas

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A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics

Cited by 42 publications

References 34 publications

Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein

Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein

Biochemical differentiation of mycelium and yeast forms of Paracoccidioides brasiliensis by Fourier transform infrared spectroscopy

Remodelamento metabólico de Paracoccidioides lutzii durante a privação de cobre determinado por análises proteômicas

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