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Elevated Activity of Dolichyl Phosphate Mannose Synthase Enhances Biocontrol Abilities of Trichoderma atroviride

December 2011 , Volume 24 , Number  12
Pages  1,522 - 1,529

Patrycja Zembek,1,2 Urszula Perlińska-Lenart,1 Kurt Brunner,2 Barbara Reithner,2 Grażyna Palamarczyk,1 Robert L. Mach,2 and Joanna S. Kruszewska1

1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland; 2Institute of Chemical Engineering, Gene Technology Group, Getreidemarkt 9/166/5/2, Vienna University of Technology, A-1060 Vienna, Austria

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Accepted 2 July 2011.

Antagonism of Trichoderma spp. against phytopathogenic fungi is widely exploited for biocontrol of plant diseases. A crucial role in the biocontrol mechanism is attributed to cell-wall-degrading enzymes secreted by Trichoderma spp. Therefore, more efficient production and secretion of the enzymes should elevate the biocontrol abilities of Trichoderma spp. Because the majority of secretory hydrolases are glycoproteins, it has been postulated that the posttranslational modification of these proteins could constitute a bottleneck in their production and secretion. Our previous study showed that improvement of O-glycosylation elevated protein secretion by Trichoderma reesei. In this study, we enhanced the biocontrol abilities of T. atroviride P1 against plant pathogens by overexpressing the Saccharomyces cerevisiae DPM1 gene coding for dolichyl phosphate mannose (DPM) synthase, a key enzyme in the O-glycosylation pathway. The transformants we obtained showed doubled DPM synthase activity and, at the same time, significantly elevated cellulolytic activity. They also revealed an improved antifungal activity against the plant pathogen Pythium ultimum.

© 2011 The American Phytopathological Society