Open AccessAf cwh41 is required for cell wall synthesis, conidiation, and polarity in Aspergillus fumigatus
Author(s) -
Zhang Lei,
Zhou Hui,
Ouyang Haomiao,
Li Yanjie,
Jin Cheng
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01376.x
Subject(s) - conidiation , aspergillus fumigatus , biology , cell wall , microbiology and biotechnology , hypha , mutant , fungal protein , hydrophobin , virulence , glycan , gene , biochemistry , glycoprotein
α‐Glucosidase I regulates trimming of the terminal α‐1,2‐glucose residue in the N‐glycan‐processing pathway, which plays an important role in the quality control system in mammalian cells. However, the consequence of glucose trimming of the N‐glycan in filamentous fungi is unclear. We identified the gene encoding α‐glucosidase I in the human opportunistic fungal pathogen Aspergillus fumigatus , namely Af cwh41 . Deletion of the Af cwh41 gene resulted in a defective N‐glycan processing of the proteins secreted by A. fumigatus . Although the Af cwh41 was not essential for hyphal growth and virulence, a severe reduction in conidia formation and a temperature‐sensitive deficiency of cell wall integrity (CWI) were observed. Also, abnormalities of polar growth and septation were observed during conidial germination and hyphal elongation of the mutant. Our results suggest that Af cwh41 was involved in CWI, polarity, septation, and conidiation in A. fumigatus , probably by affecting the proper function of the proteins that are required for cell wall synthesis.