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Afcwh41 is required for cell wall synthesis, conidiation, and polarity in Aspergillus fumigatus.

Authors
  • 1
  • 1 State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China. , (China)
Type
Published Article
Journal
FEMS microbiology letters
Publication Date
Volume
289
Issue
2
Pages
155–165
Identifiers
PMID: 19090038
Source
Medline
License
Unknown

Abstract

alpha-Glucosidase I regulates trimming of the terminal alpha-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 alpha-glucosidase I in the human opportunistic fungal pathogen Aspergillus fumigatus, namely Afcwh41. Deletion of the Afcwh41 gene resulted in a defective N-glycan processing of the proteins secreted by A. fumigatus. Although the Afcwh41 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 Afcwh41 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.

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