Journal
FUNGAL GENETICS AND BIOLOGY
Volume 128, Issue -, Pages 20-28Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2019.03.006
Keywords
Cell wall; Glycosylation; Mannan; Mannoprotein; Polarity
Categories
Funding
- National Natural Science Foundation of China [31320103901]
- Austrian Science Fund [I391]
- Austrian Science Fund (FWF) [I391] Funding Source: Austrian Science Fund (FWF)
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Owing to the essential role in protection of the Aspergillus fumigatus cell against human defense reactions, its cell wall has long been taken as a promising antifungal target. The cell wall of A. fumigatus composed of chitin, glucan and galactomannan and mannoproteins. Although galactomannan has been used as a diagnostic target for a long time, its biosynthesis remains unknown in A. fumigatus. In this study, a putative alpha 1,6-mannosyltransferase gene mnn9 was identified in A. fumigatus. Deletion of the mrtn9 gene resulted in an increased sensitivity to calcofluor white, Congo red, or hygromycin B as well as in reduced cell wall components and abnormal polarity. Although there was no major effect on N-glycan synthesis, covalently-linked cell wall mannoprotein Mp1 was significantly reduced in the mutant. Based on our results, we propose that Mnn9p is a mannosyltransferase responsible for the formation of the a-mannan in cell wall mannoproteins, potentially via elongation of O-linked mannose chains.
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