Multiple Functions of Pmt1p-mediated ProteinO-Mannosylation in the Fungal Pathogen Candida albicans
Open accessAbstract
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.
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BRG1, NDT80, and GFC1 encode three transcription factors that are core regulators of biofilm development in Candida albicans.
“BRG1, NDT80, and GFC1 encode three transcription factors that are core regulators of biofilm development in C. albicans27,34.”
From The Wor2 phenotypic switching regulator controls biofilm formation in Candida auris (2026) · cites this paper as [34]
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References 57 · Cited by 161
- Authors
- Timpel, C., Strahl-Bolsinger, S., Ziegelbauer, K., & Ernst, J. F.
- Affiliations
- Heinrich Heine University Düsseldorf (DE)
- Bayer (Germany) (DE)
- Corresponding author
- Ernst, Joachim F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 273
- Issue
- 33
- Pages
- 20837-20846
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1990447388
- Cited by
- 161
- References
- 57
- Citations by year
- 2025: 3 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 2 · 2016: 8 · 2015: 3 · 2014: 5 · 2013: 6 · 2012: 4
- FWCI
- 3.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Keywords
- protein O-mannosylation, Candida albicans, fungal pathogens, O-glycosylation, hyphal morphogenesis, antifungal susceptibility, cell adhesion, chitinase, virulence, avirulence
- MeSH terms
- Alleles, Amino Acid Sequence, Animals, Base Sequence, Candida albicans, Fungal Proteins, Genetic Complementation Test, Humans, Male, Mannose, Mannosyltransferases, Molecular Sequence Data, Mutation, Tumor Cells, Cultured, Virulence, Sequence Homology, Amino Acid, DNA Primers, Mice
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