α-(1,4)-Amylase, but not α- and β-(1,3)-glucanases, may be responsible for the impaired growth and morphogenesis of Paracoccidioides brasiliensis induced by N-glycosylation inhibition
Article first published online: 28 NOV 2013
© 2013 The Authors. Yeast published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 31, Issue 1, pages 1–11, January 2014
How to Cite
Dos Reis Almeida, F. B., Pigosso, L. L., de Lima Damásio, A. R., Monteiro, V. N., de Almeida Soares, C. M., Silva, R. N. and Roque-Barreira, M. C. (2014), α-(1,4)-Amylase, but not α- and β-(1,3)-glucanases, may be responsible for the impaired growth and morphogenesis of Paracoccidioides brasiliensis induced by N-glycosylation inhibition. Yeast, 31: 1–11. doi: 10.1002/yea.2983
- Issue published online: 7 JAN 2014
- Article first published online: 28 NOV 2013
- Accepted manuscript online: 23 OCT 2013 09:32AM EST
- Manuscript Accepted: 10 OCT 2013
- Manuscript Revised: 13 AUG 2013
- Manuscript Received: 25 JUN 2013
- Fundação de Amparo à Pesquisa do Estado de São Paulo. Grant Number: 2006/60642-2, 2009/51197-3 and 2011/02169-7
- Paracoccidioides brasiliensis;
- cell wall
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-β-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 α- and β-(1,3)-glucanases and on α-(1,4)-amylase in P. brasiliensis yeast and mycelium cells. The addition of 15 µg/ml TM to the fungal cultures did not interfere with either α- or β-(1,3)-glucanase production and secretion. Moreover, incubation with TM did not alter α- and β-(1,3)-glucanase activity in yeast and mycelium cell extracts. In contrast, α-(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 α-(1,4)-amylase activity involved in the production of malto-oligosaccharides that act as primer molecules for the biosynthesis of α-(1,3)-glucan. Our results suggest that reduced fungal α-(1,4)-amylase activity affects cell wall composition and may account for the impaired growth of underglycosylated yeast and mycelium cells. © 2013 The Authors. Yeast published by John Wiley & Sons Ltd.