A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata
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Candida glabrata is a yeast pathogen of humans. We have established a tissue culture model to analyze the interaction of C. glabrata with macrophages. Transcript profiling of yeast ingested by macrophages reveals global changes in metabolism as well as increased expression of a gene family (YPS genes) encoding extracellular glycosylphosphatidylinositol-linked aspartyl proteases. Eight of these YPS genes are found in a cluster that is unique to C. glabrata. Genetic analysis shows that the C. glabrata YPS genes are required for cell wall integrity, adherence to mammalian cells, survival in macrophages and virulence. By monitoring the processing of a cell wall adhesin, Epa1, we also show that Yps proteases play an important role in cell wall re-modeling by removal and release of glycosylphosphatidylinositol-anchored cell wall proteins.
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A transcription profile of C. glabrata following macrophage internalization revealed the up-regulation of genes involved in gluconeogenesis, β-oxidation and glyoxylate cycle, similar to what has been described for C. albicans; moreover, a putative acetate transporter (ADY2a) appears to be induced.
“A transcription profile of C. glabrata following macrophage internalization revealed the up-regulation of genes involved in gluconeogenesis, β-oxidation and glyoxylate cycle, similar to what has been described for C. albicans. Moreover, a putative acetate transporter (ADY2a) appears to be induced (Kaur et al., 2007).”
From Candida glabrata susceptibility to antifungals and phagocytosis is modulated by acetate (2015) · cites this paper as Kaur et al., 2007
C. glabrata cells resist killing by macrophages and have evolved distinct strategies for intracellular survival.
“Of note, C. glabrata cells also resist killing by macrophages and have evolved distinct strategies for intracellular survival (Otto and Howard, 1976; Kaur et al., 2007; Seider et al., 2010).”
From Candida glabrata susceptibility to antifungals and phagocytosis is modulated by acetate (2015) · cites this paper as Kaur et al., 2007
Previous studies reported ADY2a upregulation in C. glabrata cells upon macrophage phagocytosis.
“Of note, previous studies reported an ADY2a upregulation in C. glabrata cells upon macrophage phagocytosis (Kaur et al., 2007; Seider et al., 2011).”
From Candida glabrata susceptibility to antifungals and phagocytosis is modulated by acetate (2015) · cites this paper as Kaur et al., 2007
Inside phagosomes, C. glabrata faces glucose-limited environments and must change its metabolism to utilize non-fermentable carbon sources.
“In such niches, for example inside phagosomes, it faces glucose-limited environments. To survive, it has to change its metabolism and utilize non-fermentable carbon sources (Kaur et al., 2007; Roetzer et al., 2010; Fukuda et al., 2013).”
From Candida glabrata susceptibility to antifungals and phagocytosis is modulated by acetate (2015) · cites this paper as Kaur et al., 2007
The glyoxylate cycle is significant in the virulence of C. albicans and C. glabrata, and ADY2 and FPS1 are expressed inside macrophages.
“As previously mentioned, some studies have recognized the significance of the glyoxylate cycle in the virulence of C. albicans (Ramirez and Lorenz, 2007) and C. glabrata (Kaur et al., 2007; Fukuda et al., 2013) and have shown that ADY2 and FPS1 are expressed inside macrophages (Kaur et al., 2007; Seider et al., 2011).”
From Candida glabrata susceptibility to antifungals and phagocytosis is modulated by acetate (2015) · cites this paper as Kaur et al., 2007
CgYPS genes are regulated by various environmental conditions including low pH, thermal stress, macrophage and neutrophil internalization.
“CgYPS genes have been shown to be regulated by various environmental conditions including low pH, thermal stress, macrophage and neutrophil internalization [60,61,62,63].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
Despite the lack of any secreted proteolytic activity, the C. glabrata genome contains eleven genes (CgYPS1-11) that code for a family of eleven putative GPI-anchored aspartyl proteases known as Yapsins.
“However, despite the lack of any secreted proteolytic activity [59], the C. glabrata genome contains eleven genes (CgYPS1-11) that code for a family of eleven putative GPI-anchored aspartyl proteases, known as Yapsins [60].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
CgYapsins are pivotal to the regulation of several cellular processes such as maintenance of the cell wall architecture, pH and vacuole homeostasis, biofilm formation and interaction with the host.
“Consistently, CgYapsins are pivotal to the regulation of several cellular processes such as maintenance of the cell wall architecture, pH and vacuole homeostasis, biofilm formation and interaction with the host [58,60,61,64].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
CgYapsins suppress production of pro-inflammatory cytokine IL-1β in human THP-1 macrophages, facilitate survival in macrophages and virulence in the models of murine systemic candidiasis and Drosophila melanogaster.
“The latter includes suppression of the production of pro-inflammatory cytokine IL-1β in human THP-1 macrophages, facilitating survival in macrophages and virulence in the models of murine systemic candidiasis and Drosophila melanogaster [58,60,65,66].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
CgYapsins are implicated in shedding Epa1 adhesin off the cell wall; Epa1 release into the medium was drastically reduced in the Cgyps1-11Δ mutant compared to wild-type cells.
“CgYapsins have also been implicated in shedding Epa1 adhesin off the cell wall, as Epa1 release into the medium was drastically reduced in the Cgyps1-11Δ mutant compared to wild-type cells (Figure 1) [60].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
C. glabrata survives and replicates in human and murine macrophages without adversely affecting macrophages.
“C. glabrata survives and replicates in human and murine macrophages without adversely affecting macrophages [60,65,147].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
Genes encoding glycolytic enzymes and ribosomal translational machinery components are downregulated in macrophage-internalized C. glabrata cells.
“Genes belonging to the glyoxylate cycle, β-oxidation of fatty acids, gluconeogenesis, methyl citrate cycle and proteolysis have been shown to be upregulated, while genes encoding glycolytic enzymes and ribosomal translational machinery components were found to be downregulated in macrophage-internalized C. glabrata cells [60].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
Genes belonging to the glyoxylate cycle, β-oxidation of fatty acids, gluconeogenesis, methyl citrate cycle, and proteolysis are upregulated in macrophage-internalized C. glabrata cells.
“Genes belonging to the glyoxylate cycle, β-oxidation of fatty acids, gluconeogenesis, methyl citrate cycle and proteolysis have been shown to be upregulated, while genes encoding glycolytic enzymes and ribosomal translational machinery components were found to be downregulated in macrophage-internalized C. glabrata cells [60].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
C. glabrata has equipped itself with strategies to proliferate in macrophages, including transcriptional reconfiguration of cellular pathways.
“Lastly, despite encountering iron restriction, ROS and carbon starvation, C. glabrata has equipped itself well with strategies to proliferate in macrophages, including transcriptional reconfiguration of cellular pathways [60,65,147].”
From Candida glabrata: A Lot More Than Meets the Eye (2019) · cites this paper as [60]
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- Authors
- Kaur, R., Ma, B., & Cormack, B. P.
- Affiliations
- Johns Hopkins University (US)
- Electronics Corporation of India (IN)
- Corresponding author
- Cormack, Brendan P.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-05
- Volume
- 104
- Issue
- 18
- Pages
- 7628-7633
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1863504
- OpenAlex
- W2100246797
- Cited by
- 284
- References
- 23
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 12 · 2023: 11 · 2022: 19 · 2021: 14 · 2020: 16 · 2019: 17 · 2018: 14 · 2017: 12 · 2016: 10 · 2015: 18 · 2014: 23 · 2013: 25 · 2012: 19
- FWCI
- 4.64
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Johns Hopkins University
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI046223)
- 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 glabrata, virulence, macrophage survival, cell wall integrity, cell wall remodeling, cell adhesion, gene expression profiling, fungal pathogens
- MeSH terms
- Animals, Candidiasis, Cell Line, Macrophages, Mice, Inbred BALB C, Mutation, Protein Binding, Substrate Specificity, Virulence, Up-Regulation, Aspartic Acid Endopeptidases, Glycosylphosphatidylinositols, Gene Deletion, Candida glabrata, Mice
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