Binding of Paracoccidioides brasiliensis to laminin through surface glycoprotein gp43 leads to enhancement of fungal pathogenesis.
AUTOR(ES)
Vicentini, A P
RESUMO
Extracellular matrix protein laminin binds specifically to yeast forms of Paracoccidioides brasiliensis and enhances adhesion of the fungus to the surface of epithelial Madin-Darby canine kidney cells in vitro. Immunoblotting of fungal extracts showed that the gp43 glycoprotein is responsible for adhesion. This was confirmed by binding assays using purified gp43, with a Kd of 3.7 nM. The coating of P. brasiliensis yeast forms with laminin before injection into hamster testicles enhanced the fungus virulence, resulting in a faster and more severe granulomatous disease. These results indicate that interaction of fungi with extracellular matrix elements may constitute a basis for the evolution of fungal infection toward regional spreading and dissemination.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=186304Documentos Relacionados
- Avaliação da resposta linfoproliferativa de pacientes com paracoccidioidomicose e indivíduos curados a antígenos de Paracoccidioides brasiliensis: filtrado de cultura, gp43 e gp43 tratada com metaperiodato
- Variable gp43 Secretion by Paracoccidioides brasiliensis Clones Obtained by Two Different Culture Methods
- Immune protection by dendritic cells pulsed with peptide P10 derived from the gp43 of Paracoccidioides brasiliensis.
- Obtenção de gp43 de Paracoccidioides brasiliensis recombinante em Escherichia coli e produção de anticorpos policlonais para gp43 em galinhas poedeiras imunizadas com vacina de DNA
- Polymorphism in the Gene Coding for the Immunodominant Antigen gp43 from the Pathogenic Fungus Paracoccidioides brasiliensis