alpha-(1,4)-Amylase, but not alpha- and beta-(1,3)-glucanases, may be responsible for the impaired growth and morphogenesis of Paracoccidioides brasiliensis induced by N-glycosylation inhibition

Autor(es)

Dos Reis Almeida, Fausto Bruno ^[1] ; Pigosso, Laurine Lacerda ^[2] ; de Lima Damasio, Andre Ricardo ^[3] ; Monteiro, Valdirene Neves ^[4] ; de Almeida Soares, Celia Maria ^[2] ; Silva, Roberto Nascimento ^[5] ; Roque-Barreira, Maria Cristina ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, BR-14049900 Ribeirao Preto, SP - Brazil

^[2] Univ Fed Goias, Inst Ciencias Biol, Lab Biol Mol, Goiania, Go - Brazil

^[3] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Ciencia & Tecnol Bioetanol, Campinas, SP - Brazil

^[4] Univ Estadual Goias, UnUCET, BR-75000000 Anapolis, Go - Brazil

^[5] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, BR-14040900 Ribeirao Preto, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: YEAST; v. 31, n. 1, p. 1-11, JAN 2014.
• Citações Web of Science: 7

Resumo

The cell wall of Paracoccidioides brasiliensis, which consists of a network of polysaccharides and glycoproteins, is essential for fungal pathogenesis. We have previously reported that N-glycosylation of proteins such as N-acetyl-beta-d-glucosaminidase is required for the growth and morphogenesis of P. brasiliensis. In the present study, we investigated the influence of tunycamicin (TM)-mediated inhibition of N-linked glycosylation on alpha- and beta-(1,3)-glucanases and on alpha-(1,4)-amylase in P. brasiliensis yeast and mycelium cells. The addition of 15 mu g/ml TM to the fungal cultures did not interfere with either alpha- or beta-(1,3)-glucanase production and secretion. Moreover, incubation with TM did not alter alpha- and beta-(1,3)-glucanase activity in yeast and mycelium cell extracts. In contrast, alpha-(1,4)-amylase activity was significantly reduced in underglycosylated yeast and mycelium extracts after exposure to TM. In spite of its importance for fungal growth and morphogenesis, N-glycosylation was not required for glucanase activities. This is surprising because these activities are directed to wall components that are crucial for fungal morphogenesis. On the other hand, N-glycans were essential for alpha-(1,4)-amylase activity involved in the production of malto-oligosaccharides that act as primer molecules for the biosynthesis of alpha-(1,3)-glucan. Our results suggest that reduced fungal alpha-(1,4)-amylase activity affects cell wall composition and may account for the impaired growth of underglycosylated yeast and mycelium cells. (c) 2013 The Authors. Yeast published by John Wiley \& Sons Ltd. (AU)

• Processo FAPESP: 11/02169-7 - Aspergillus nidulans como modelo para expressão heteróloga de celulases e hemicelulases
• Beneficiário: André Ricardo de Lima Damasio
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 06/60642-2 - Efeitos biológicos e aplicações farmacêuticas de lectinas
• Beneficiário: Maria Cristina Roque Antunes Barreira
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 09/51197-3 - Papel de N-glicanas em atividades desempenhadas por paracoccina
• Beneficiário: Fausto Bruno dos Reis Almeida
• Modalidade de apoio: Bolsas no Brasil - Doutorado