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Published on: February 14, 2011
Binding of extracellular matrix proteins to Paracoccidioides brasiliensis
Maria José Soares Mendes-Giannini1, Patrícia Ferrari Andreotti, Luciana Raquel Vincenzi
1Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, UNESP, R. Expedicionários do Brasil, 1621, 14802-901 Araraquara São Paulo, Brazil. giannini@fcfar.unesp.br
Abstract:
Adhesion to extracellular matrix (ECM) proteins plays a crucial role in invasive fungal diseases. ECM proteins bind to the surface of Paracoccidioides brasiliensis yeast cells in distinct qualitative patterns. Extracts from Pb18 strain, before (18a) and after animal inoculation (18b), exhibited differential adhesion to ECM components. Pb18b extract had a higher capacity for binding to ECM components than Pb18a. Laminin was the most adherent component for both samples, followed by type I collagen, fibronectin, and type IV collagen for Pb18b. A remarkable difference was seen in the interaction of the two extracts with fibronectin and their fragments. Pb18b extract interacted significantly with the 120-kDa fragment. Ligand affinity binding assays showed that type I collagen recognized two components (47 and 80kDa) and gp43 bound both fibronectin and laminin. The peptide 1 (NLGRDAKRHL) from gp43, with several positively charged amino acids, contributed most to the adhesion of P. brasiliensis to Vero cells. Synthetic peptides derived from peptide YIGRS of laminin or from RGD of both laminin and fibronectin showed the greatest inhibition of adhesion of gp43 to Vero cells. In conclusion, this work provided new molecular details on the interaction between P. brasiliensis and ECM components.
Insights
Invasive fungal diseases involve fungal cell adhesion to extracellular matrix (ECM) proteins. This study details molecular interactions between Paracoccidioides brasiliensis and ECM, revealing key adhesion mechanisms.
Area of Science:
- Microbiology
- Mycology
- Infectious Diseases
Background:
- Adhesion to extracellular matrix (ECM) proteins is vital for invasive fungal infections.
- Paracoccidioides brasiliensis yeast cells exhibit specific binding patterns to ECM components.
Purpose of the Study:
- To investigate the differential adhesion of Paracoccidioides brasiliensis extracts to ECM proteins.
- To identify molecular components and interactions involved in fungal adhesion.
Main Methods:
- Comparison of ECM binding by fungal extracts before and after animal inoculation.
- Ligand affinity binding assays to characterize protein interactions.
- Inhibition assays using synthetic peptides to block adhesion.
Main Results:
- Fungal extracts after animal inoculation showed enhanced ECM binding, particularly to laminin and type I collagen.
- Specific interactions were observed between fungal components and fibronectin fragments.
- The gp43 protein and its peptide 1 were identified as key contributors to fungal adhesion.
- Synthetic peptides targeting laminin and fibronectin significantly inhibited fungal adhesion.
Conclusions:
- This research elucidates novel molecular details of the interaction between Paracoccidioides brasiliensis and ECM.
- Understanding these interactions can inform strategies for combating invasive fungal diseases.
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