title: Binding of extracellular matrix proteins to Paracoccidioides brasiliensis.
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.
authors.affiliation: Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, UNESP, R. Expedicionários do Brasil, 1621, 14802-901 Araraquara São Paulo, Brazil. giannini@fcfar.unesp.br
authors.forename: Maria José Soares
authors.initials: MJ
authors.lastname: Mendes-Giannini
authors.forename: Patrícia Ferrari
authors.initials: PF
authors.lastname: Andreotti
authors.forename: Luciana Raquel
authors.initials: LR
authors.lastname: Vincenzi
authors.forename: Juliana Leal Monteiro
authors.initials: JL
authors.lastname: da Silva
authors.forename: Henrique Leonel
authors.initials: HL
authors.lastname: Lenzi
authors.forename: Gil
authors.initials: G
authors.lastname: Benard
authors.forename: Roseli
authors.initials: R
authors.lastname: Zancopé-Oliveira
authors.forename: Herbert Leonel
authors.initials: HL
authors.lastname: de Matos Guedes
authors.forename: Christiane Pienna
authors.initials: CP
authors.lastname: Soares
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000946:Antigens, Fungal / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology; D002522:Chlorocebus aethiops; D004797:Enzyme-Linked Immunosorbent Assay; D005109:Extracellular Matrix / Q000378:metabolism / Q000382:microbiology*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005434:Flow Cytometry; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010228:Paracoccidioides / Q000235:genetics / Q000378:metabolism*; D010229:Paracoccidioidomycosis / Q000378:metabolism / Q000382:microbiology*; D010446:Peptide Fragments / Q000378:metabolism; D016415:Sequence Alignment; D014709:Vero Cells
chemical_list: C103180:43 kDa protein, Paracoccidioides; D000946:Antigens, Fungal; D016326:Extracellular Matrix Proteins; D005656:Fungal Proteins; D006023:Glycoproteins; D010446:Peptide Fragments