Fausto Almeida, Amanda Cristina Campos Antoniêto, André Moreira Pessoni, Valdirene Neves Monteiro, Ana Claudia Paiva Alegre-Maller, Laurine Lacerda Pigosso, Maristela Pereira, Célia Maria de Almeida Soares and Maria Cristina Roque-Barreira Pages 112 - 118 ( 7 )
Paracoccidioidomycosis is the most prevalent systemic mycosis in Latin America. It is caused by the temperature- dependent dimorphic fungus Paracoccidioides brasiliensis. The P. brasiliensis cell wall is a dynamic outer structure, composed of a network of glycoproteins and polysaccharides, such as chitin, glucan and N-glycosylated proteins. These glycoproteins can interact with the host to affect infection rates, and are known to perform other functions. We inhibited N-linked glycosylation using tunicamycin (TM), and then evaluated the expression of P. brasiliensis genes related to cell wall remodeling. Our results suggest that cell wall synthesis related genes, such as β-1,3-glucanosyltransferase (PbGEL3), 1,3-β-D-glucan synthase (PbFKS1), and α-1,4-amylase (PbAMY), as well as cell wall degrading related genes, such as Nacetyl- β-D-glucosaminidase (PbNAG1), α-1,3-glucanase (PbAGN), and β-1,3-glucanase (PbBGN1 and PbBGN2), have their expression increased by the N-glycosylation inhibition, as detected by qRT-PCR. The observed increases in gene expression levels reveal possible compensatory mechanisms for diminished enzyme activity due to the lack of glycosylation caused by TM.
N-glycan, Paracoccidioides brasiliensis, Cell wall, Fungal cell.
Departamento de Biologia Celular e Molecular e Bioagentes Patogênicos, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Av. Bandeirantes 3900, Ribeirão Preto, SP 14049-900, Brazil.