| Full text | |
| Author(s): |
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
|
| Affiliation: | [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 |
| Abstract | |
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 Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 06/60642-2 - Lectins: biological effects and pharmaceutical applications |
| Grantee: | Maria Cristina Roque Antunes Barreira |
| Support Opportunities: | 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 Opportunities: | Scholarships in Brazil - Doctorate |