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J Biol Chem, Vol. 273, Issue 33, 20837-20846, August 14, 1998
,
From the Protein mannosylation by Pmt proteins initiates
O-glycosylation in fungi. We have identified the
PMT1 gene and analyzed the function of Pmt1p in the fungal
human pathogen Candida albicans. Mutants defective in
PMT1 alleles lacked Pmt in vitro enzymatic activity, showed reduced growth rates, and tended to form cellular aggregates. In addition, multiple specific deficiencies not known in
Saccharomyces cerevisiae (including defective hyphal
morphogenesis; supersensitivity to the antifungal agents hygromycin B,
G418, clotrimazole, and calcofluor white; and reduced adherence to
Caco-2 epithelial cells) were observed in pmt1 mutants.
PMT1 deficiency also led to faster electrophoretic mobility
of the Als1p cell wall protein and to elevated extracellular activities
of chitinase. Homozygous pmt1 mutants were avirulent in a
mouse model of systemic infection, while heterozygous
PMT1/pmt1 strains showed reduced virulence. The
results indicate that protein O-mannosylation by Pmt
proteins occurs in different fungal species, where PMT1
deficiency can lead to defects in multiple cellular functions.
Institut für Mikrobiologie und
Biologisch-Medizinisches Forschungszentrum,
Heinrich-Heine-Universität, D-40225 Düsseldorf,
Germany, § Lehrstuhl für Zellbiologie und
Pflanzenphysiologie, Universität Regensburg, 93040 Regensburg,
Germany, and the ¶ Institute for Antiinfectiva Research, Bayer
AG, 42117 Wuppertal, Germany
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