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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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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]
Total Authors: 7
[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
Total Affiliations: 5
Document type: Journal article
Source: YEAST; v. 31, n. 1, p. 1-11, JAN 2014.
Web of Science Citations: 7

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)

FAPESP's process: 11/02169-7 - Aspergillus nidulans as a model for heterologous expression of cellulases and hemicellulases
Grantee:André Ricardo de Lima Damasio
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 06/60642-2 - Lectins: biological effects and pharmaceutical applications
Grantee:Maria Cristina Roque Antunes Barreira
Support type: Research Projects - Thematic Grants
FAPESP's process: 09/51197-3 - Role of N-glycans in activities developed by paracoccin
Grantee:Fausto Bruno dos Reis Almeida
Support type: Scholarships in Brazil - Doctorate