Candida glabrata Pwp7p and Aed1p are required for adherence to human endothelial cells: Candida glabrata adhesins
Open accessAbstract
Candida glabrata owes its success as a pathogen, in part, to a large repertoire of adhesins present on the cell surface. Our current knowledge of C. glabrata adhesins and their role in the interaction between host and pathogen is limited to work with only a single family of epithelial adhesins (Epa proteins). Here, we report on the identification and characterization of a family of glycosylphosphatidylinositol-anchored cell wall proteins in C. glabrata. These proteins are absent in both Saccharomyces cerevisiae and Candida albicans, suggesting that C. glabrata has evolved different mechanism(s) for interaction with host cells. In the current study, we present data on the characterization of Pwp7p (PA14 domain containing Wall Protein) and Aed1p (Adherence to Endothelial cells) of this family in the interaction of C. glabrata with human umbilical vein endothelial cells. The deletion of C. glabrata genes PWP7 and AED1 results in a significant reduction in adherence to endothelial cells compared with the wild-type parent. These data indicate that C. glabrata utilizes these proteins for adherence to endothelial cells in vitro.
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C. glabrata possesses a set of 337 genes that are absent in S. cerevisiae.
“Consistently, C. glabrata contains orthologs of 4870 S. cerevisiae genes [https://yeastmine.yeastgenome.org/], however, it also possesses a set of 337 genes that are absent in S. cerevisiae [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
Aed1, belonging to sub-family III, has been implicated in adherence to human endothelial cells.
“One such protein, Aed1 (Adherence to Endothelial cells), belonging to the sub-family III, has been implicated in adherence to human endothelial cells [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
Pwp7 protein is required for adherence to human endothelial cells in vitro.
“Of these Pwp1-7, the Pwp7 protein is required for adherence to human endothelial cells in vitro [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
CgPWP7 and CgAED1 are not transcriptionally regulated by silencing.
“However, unlike EPA genes, CgPWP7 and CgAED1 were not transcriptionally regulated by silencing [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
Mutants lacking CgPwp7 and CgAed1 were 2-3-fold less adherent to HUVEC.
“Furthermore, two GPI-anchored cell wall proteins, CgPwp7 and CgAed1, have been shown to be required for adherence to HUVEC, as mutants lacking these adhesins were 2-3-fold less adherent [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
CgPwp7 and CgAed1 are required for adherence to HUVEC.
“Furthermore, two GPI-anchored cell wall proteins, CgPwp7 and CgAed1, have been shown to be required for adherence to HUVEC, as mutants lacking these adhesins were 2-3-fold less adherent [23].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [23]
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- Authors
- Desai, C., Mavrianos, J., & Chauhan, N.
- Affiliations
- Rutgers New Jersey Medical School (US)
- Corresponding author
- Chauhan, Neeraj
- Venue
- FEMS Yeast Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-07-29
- Volume
- 11
- Issue
- 7
- Pages
- 595-601
- ISSN
- 1567-1356 (ISSN-L)
- PMC
- PMC3202042
- OpenAlex
- W2138145776
- Cited by
- 52
- References
- 35
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 4 · 2019: 3 · 2018: 5 · 2016: 2 · 2015: 7 · 2014: 2 · 2013: 5 · 2012: 4
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEMS Yeast Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- Funders
- American Heart Association
- Johns Hopkins University
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R21AI076084)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Yeasts and Rust Fungi Studies
- Keywords
- Candida glabrata, cell adhesion, endothelial cells, GPI-anchored proteins, cell wall proteins, adhesins, host-pathogen interaction, gene deletion, fungal virulence
- MeSH terms
- Candida albicans, Cell Adhesion, Cells, Cultured, Fungal Proteins, Humans, Membrane Proteins, Saccharomyces cerevisiae, Gene Deletion, Virulence Factors, Candida glabrata, Endothelial Cells
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