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Published online ahead of print on 23 April 2009 as doi:10.1099/mic.0.027490-0
Microbiology 2009;155:2157.

Microbiology (2009), DOI 10.1099/mic.0.027490-0
© 2009 Society for General Microbiology
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Microbiology 0 (2009), mic.0.027490; DOI  10.1099/mic.0.027490-0
© 2009 Society for General Microbiology

Comparative proteome analysis of the Aspergillus fumigatus mutant deficient of glucosidase I (AfCwh41)

Lei Zhang, Deqin Feng, Wenxia Fang, Haomiao Ouyang, Yuanming Luo, Ting Du and Cheng Jin1

Institute of Microbiology, Chinese Academy of Sciences

ABSTRACT

{alpha}-glucosidase I regulates trimming of the terminal {alpha}-1, 2-glucose residue in N-glycan processing pathway, which plays an important role in quality control system in mammalian cell. Previously, we identified the gene encoding for {alpha}-glucosidase I in the human opportunistic fungal pathogen Aspergillus fumigatus, namely Afcwh41. Deletion of the Afcwh41 gene results in a severe reduction of conidia formation, a temperature-sensitive deficiency of cell wall integrity, and abnormalities of polar growth and septation. Also an up-regulation of the genes encoding Rho-type GTPases is documented, which suggests an activation of the cell wall integrity pathway in the mutant. Using 2-D gel analysis, we revealed that the proteins involved in protein assembly, ubiquitin mediated degradation, and actin orgainztion were altered in the {Delta}Afcwh41 mutant. Evidence has been obtained to show a defective polarized localization of the actin cytoskeleton in the mutant. Our results suggest that blocking of the glucose-trimming in A. fumigatus might induce accumulation of misfolded proteins in the ER, probably these misfolded proteins are required for cell wall synthesis and thus activate the cell wall integrity pathway, which then causes the abnormal polarity associated with the {Delta}Afcwh41 mutant.

1 E-mail: jinc{at}sun.im.ac.cn






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