Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/5967
Title: Binding of extracellular matrix proteins to Paracoccidioides brasiliensis
Authors: Giannini, Maria José Soares Mendes
Andreotti, Patrícia Ferrari
Vincenzi, Luciana Raquel
Silva, Juliana Leal Monteiro da
Lenzi, Henrique Leonel
Benard, Gil
Oliveira, Roseli Zancopé
Guedes, Herbert Leonel de Matos
Soares, Christiane Pienna
Affilliation: Universidade Estadual Paulista. Faculdade de Ciências Farmacêuticas. Departamento de Análises Clínicas. Araraquara, São Paulo, Brasil.
Universidade Estadual Paulista. Faculdade de Ciências Farmacêuticas. Departamento de Análises Clínicas. Araraquara, São Paulo, Brasil.
Universidade Estadual Paulista. Faculdade de Ciências Farmacêuticas. Departamento de Análises Clínicas. Araraquara, São Paulo, Brasil.
Universidade Estadual Paulista. Faculdade de Ciências Farmacêuticas. Departamento de Análises Clínicas. Araraquara, São Paulo, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Patologia. Rio de Janeiro, RJ, Brasil.
Universidade de São Paulo. Faculdade de Medicina. Laboratório de Alergia e Imunologia Clínica e Experimental. São Paulo, SP, Brasil.
Fundação Oswaldo Cruz. Instituto de Pesquisa Clínica Evandro Chagas. Laboratório de Micologia. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto de Pesquisa Clínica Evandro Chagas. Laboratório de Micologia. Rio de Janeiro, RJ, Brasil.
Universidade Estadual Paulista. Faculdade de Ciências Farmacêuticas. Departamento de Análises Clínicas. Araraquara, São Paulo, Brasil.
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 80 kDa) 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.
Keywords: Paracoccidioides brasiliensis
Extracellular matrix
Adhesins
gp43
Células epiteliais
keywords: Clínica médica
Dermatopatias infecciosas
Paracoccidioidomicose
Matriz extracelular
Células epiteliais
DeCS: Medicina Clínica
Dermatopatias Infecciosas
Paracoccidioidomicose
Matriz Extracelular
Adesinas Bacterianas
Issue Date: 2006
Publisher: Elsevier
Citation: ANDREOTTI, P. F. et. al. Binding of extracellular matrix proteins to Paracoccidioides brasiliensis. Microbes and Infection, v. 8, p. 1550-1559, 2006.
DOI: http://dx.doi.org/10.1016/j.micinf.2006.01.012
ISSN: 1286-4579
Copyright: open access
Appears in Collections:INI - Artigos de Periódicos
IOC - Artigos de Periódicos

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