Identification of proteins highly expressed in the hyphae of <i>Candida albicans</i> by two‐dimensional electrophoresis

Yoo, Yung Joon; Kim, Minkyoung; Shin, Duckhyang; Jeon, Hong Bae; Choi, Won‐Young

doi:10.1002/yea.1022

Cited by 40 publications

(37 citation statements)

References 20 publications

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“…6A, top right panel). Cell wall localization has already been reported through biochemical analysis of cell wall extracts (12). It should be noted that cell morphology is pseudohyphal when grown in this medium, compared to the yeastlike morphology when cells are grown in YPD at the same temperature (not shown).…”

Section: Resultsmentioning

confidence: 61%

“…Among such genes, we noted PRA1 to be highly upregulated. Pra1p is a cell wall-associated protein found in both the yeast and hyphal forms of C. albicans: Pra1p becomes highly glycosylated in hyphal-form cells (12) and elicits a strong immune response in infected patients (77). Pra1p was also identified as mp58 (58-kDa mannoprotein) or Fbp1 (fibrinogen binding protein) (45,78).…”

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confidence: 99%

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Analysis ofPRA1and Its Relationship toCandida albicans- Macrophage Interactions

et al. 2008

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Phagocytosis of Candida albicans by either primary bone marrow-derived mouse macrophages or RAW 264.7 cells upregulated transcription of PRA1, which encodes a cell wall/membrane-associated antigen previously described as a fibrinogen binding protein. However, a pra1 null mutant was still able to bind fibrinogen, showing that Pra1p is not uniquely required for fibrinogen binding. As well, Pra1 tagged with green fluorescent protein did not colocalize with AlexaFluor 546-labeled human fibrinogen, and while PRA1 expression was inhibited when Candida was grown in fetal bovine serum-containing medium, Candida binding to fibrinogen was activated by these conditions. Therefore, it appears that Pra1p can play at most a minor role in fibrinogen binding to C. albicans. PRA1 gene expression is induced in vitro by alkaline pH, and therefore its activation in phagosomes suggested that phagosome maturation was suppressed by the presence of Candida cells. LysoTracker red-labeled organelles failed to fuse with phagosomes containing live Candida, while phagosomes containing dead Candida underwent a normal phagosome-to-phagolysosome maturation. Immunofluorescence staining with the early/recycling endosomal marker transferrin receptor (CD71) suggested that live Candida may escape macrophage destruction through the inhibition of phagolysosomal maturation.

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Section: Resultsmentioning

confidence: 61%

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confidence: 99%

Analysis ofPRA1and Its Relationship toCandida albicans- Macrophage Interactions

et al. 2008

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“…In parallel, several C. albicans cell wall proteins have been shown to play an important role in pathogenesis or cell wall organization/remodeling. Most of these proteins display glycosylation sites but the chemical nature of the mannose oligomers attached is unknown, contrasting with recent studies indicating that cell wall protein post-translational modifications caused by variable glycosylation can control transcription (48). The second issue is the observation of ␤-1,2 oligomannoside epitope overexpression on mannoproteins at pH 2.0 in the absence of PLM.…”

Section: Fig 4 Mit1 Deletion Does Not Affect Cell Morphogenesismentioning

confidence: 82%

Inactivation of CaMIT1 Inhibits Candida albicans Phospholipomannan β-Mannosylation, Reduces Virulence, and Alters Cell Wall Protein β-Mannosylation

Mille

Janbon

Delplace

et al. 2004

Journal of Biological Chemistry

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Studies on Candida albicans phospholipomannan have suggested a novel biosynthetic pathway for yeast glycosphingolipids. This pathway is thought to diverge from the usual pathway at the mannose-inositol-phospho-ceramide (MIPC) step. To confirm this hypothesis, a C. albicans gene homologue for the Saccharomyces cerevisiae SUR1 gene was identified and named MIT1 as it coded for GDP-mannose:inositol-phospho-ceramide mannose transferase. Two copies of this gene were disrupted. Western blots of cell extracts revealed that strain mit1⌬ contained no PLM. Thin layer chromatography and mass spectrometry confirmed that mit1⌬ did not synthesize MIPC, demonstrating a role of MIT1 in the mannosylation of C. albicans IPCs. As MIT1 disruption prevented downstream ␤-1,2 mannosylation, mit1⌬ represents a new C. albicans mutant affected in the expression of these specific virulence attributes, which act as adhesins/immunomodulators. mit1⌬ was less virulent during both the acute and chronic phases of systemic infection in mice (75 and 50% reduction in mortality, respectively). In vitro, mit1⌬ was not able to escape macrophage lysis through down-regulation of the ERK1/2 phosphorylation pathway previously shown to be triggered by PLM. Phenotypic analysis also revealed pleiotropic effects of MIT1 disruption. The most striking observation was a reduced ␤-mannosylation of phosphopeptidomannan. Increased ␤-mannosylation of mannoproteins was observed under growth conditions that prevented the association of ␤-oligomannosides with phosphopeptidomannan, but not with PLM. This suggests that C. albicans has strong regulatory mechanisms associating ␤-oligomannoses with different cell wall carrier molecules. These mechanisms and the impact of the different presentations of ␤-oligomannoses on the host response need to be defined.

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“…In a proteomic study, three of six spots that were more abundant in a silver-stained gel of hyphal whole-cell lysates were identified as Pra1p (58). Two of the spots were identified as Phr1p.…”

Section: Adhesinsmentioning

confidence: 99%

Candida albicansCell Wall Proteins

Chaffin

2008

Microbiol Mol Biol Rev

435

404

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SUMMARY The Candida albicans cell wall maintains the structural integrity of the organism in addtion to providing a physical contact interface with the environment. The major components of the cell wall are fibrillar polysaccharides and proteins. The proteins of the cell wall are the focus of this review. Three classes of proteins are present in the candidal cell wall. One group of proteins attach to the cell wall via a glycophosphatidylinositol remnant or by an alkali-labile linkage. A second group of proteins with N-terminal signal sequences but no covalent attachment sequences are secreted by the classical secretory pathway. These proteins may end up in the cell wall or in the extracellular space. The third group of proteins lack a secretory signal, and the pathway(s) by which they become associated with the surface is unknown. Potential constituents of the first two classes have been predicted from analysis of genome sequences. Experimental analyses have identified members of all three classes. Some members of each class selected for consideration of confirmed or proposed function, phenotypic analysis of a mutant, and regulation by growth conditions and transcription factors are discussed in more detail.

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Identification of proteins highly expressed in the hyphae of Candida albicans by two‐dimensional electrophoresis

Cited by 40 publications

References 20 publications

Analysis ofPRA1and Its Relationship toCandida albicans- Macrophage Interactions

Analysis ofPRA1and Its Relationship toCandida albicans- Macrophage Interactions

Inactivation of CaMIT1 Inhibits Candida albicans Phospholipomannan β-Mannosylation, Reduces Virulence, and Alters Cell Wall Protein β-Mannosylation

Candida albicansCell Wall Proteins

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