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Eukaryotic Cell, December 2007, p. 2260-2268, Vol. 6, No. 12
1535-9778/07/$08.00+0 doi:10.1128/EC.00261-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Hongyan Hu,2,
Lijuan Zhang,3
Ruoyu Li,3
Haomiao Ouyang,1
Jia Ming,1 and
Cheng Jin1*
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China,1 The General Hospital of Chinese People's Armed Police Forces, Beijing, China,2 Research Center for Medical Mycology, Peking University First Hospital, Peking University, Beijing 100034, China3
Received 20 July 2007/ Accepted 12 September 2007
Protein O-mannosyltransferases initiate O mannosylation of secretory proteins, which are of fundamental importance in eukaryotes. In this study, the PMT gene family of the human fungal pathogen Aspergillus fumigatus was identified and characterized. Unlike the case in Saccharomyces cerevisiae, where the PMT family is highly redundant, only one member of each PMT subfamily, namely, Afpmt1, Afpmt2, and Afpmt4, is present in A. fumigatus. Mutants with a deletion of Afpmt1 are viable. In vitro and in vivo activity assays confirmed that the protein encoded by Afpmt1 acts as an O-mannosyltransferase (AfPmt1p). Characterization of the
Afpmt1 mutant showed that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 was not required for the virulence of A. fumigatus under the experimental conditions used.
Published ahead of print on 28 September 2007.
H.Z. and H.H. made equal contributions to this work.
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