Insight into the Antiadhesive Effect of Yeast Wall Protein 1 of Candida albicans
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Ywp1 is a prominent glycosylphosphatidylinositol (GPI)-anchored glycoprotein of the cell wall of Candida albicans ; it is present in the yeast form of this opportunistic fungal pathogen but absent from filamentous forms and chlamydospores. Yeast cells that lack Ywp1 are more adhesive and form thicker biofilms, implying an antiadhesive activity for Ywp1, with a possible role in yeast dispersal. The antiadhesive effect of Ywp1 is transplantable from yeast to hyphae, as hyphae that are forced to express YWP1 lose adhesion in an in vitro assay. Deletion of the GPI anchor results in loss of Ywp1 to the surrounding medium and reduction of the antiadhesive effect, implying an importance of time-dependent residency in the cell wall. Anchor-negative versions of Ywp1 possessing or lacking a C-terminal green fluorescent protein (GFP) tag were created in C. albicans and harvested from culture supernatants; in addition to serving as quantifiable markers for Ywp1 secretion, they revealed that the cleaved 11-kDa propeptide of Ywp1 remains strongly but noncovalently associated with the Ywp1 core. This association is resistant to highly acidic and basic solutions, 8 M urea, and 1% SDS (below 45°C). Above 50°C, SDS dissociates the isolated complex, but even higher temperatures are required to dissociate the propeptide from native Ywp1 that is anchored in a cell wall. This property has permitted detection, for the first time, of orthologs of Ywp1 in other members of the Candida clade. The cleaved propeptide, which carries the sole N-glycan of Ywp1, must participate in the antiadhesive effect of Ywp1.
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Deletion of YWP1 leads to decreased biofilm dispersal and increased biofilm adhesiveness.
“The cell wall protein Ywp1 is also important for biofilm dispersal, as deletion of YWP1 leads to decreased biofilm dispersal and increased biofilm adhesiveness (69, 70).”
From <i>Candida albicans</i> Biofilms and Human Disease (2015) · cites this paper as [69]
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- Authors
- Granger, B. L.
- Affiliations
- Montana State University (US)
- Corresponding author
- Granger, Bruce L.
- ORCID
- Granger, Bruce L.
- Venue
- Eukaryotic Cell
- Publisher
- American Society for Microbiology
- Published
- 2012-06
- Volume
- 11
- Issue
- 6
- Pages
- 795-805
- ISSN
- 1535-9778 (ISSN-L)
- 1535-9786
- PMC
- PMC3370456
- OpenAlex
- W2131070633
- Cited by
- 48
- References
- 71
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 2 · 2022: 3 · 2021: 3 · 2020: 5 · 2019: 5 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 4 · 2013: 1
- FWCI
- 0.64
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Eukaryotic Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Iowa State University
- Montana State University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Keywords
- Candida albicans, adhesion prevention, yeast adhesion, biofilm formation, glycosylphosphatidylinositol anchoring, cell wall proteins, hyphal adhesion, propeptide, N-glycans, protein secretion, fungal pathogens
- MeSH terms
- Amino Acid Sequence, Animals, Candida albicans, Cell Adhesion, Cell Line, Cell Wall, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Humans, Models, Biological, Molecular Sequence Data, Peptides, Recombinant Fusion Proteins, Blotting, Western, Sequence Homology, Amino Acid, Biofilms, Hyphae, Green Fluorescent Proteins
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