Comprehensive Analysis of Glycosylphosphatidylinositol-Anchored Proteins in
            <i>Candida albicans</i>

Richard, Mathias L.; Plaine, Armêl

doi:10.1128/ec.00297-06

Cited by 143 publications

(161 citation statements)

References 65 publications

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“…As in C. albicans predictions about the localization of GPImodified proteins based on the amino acid environment upstream of the v site do not always match the experimental data (Richard & Plaine, 2007), we decided to experimentally localize Pga59 and Pga62. For this purpose, plasmids carrying PGA59-GFP and PGA62-GFP gene fusions were constructed by cloning the GFP coding region immediately downstream of the codons corresponding to the second amino acid in the mature Pga59 or Pga62 protein, respectively ( Fig.…”

Section: Pga59 and Pga62 Are Cell Wall Proteinsmentioning

confidence: 99%

“…Most proteins in the cell wall of ascomycetous yeasts are glycosylphosphatidylinositolanchored proteins (GPI-modified proteins) that become covalently linked to b-1,6-glucan through a remnant of their GPI anchor. As the b-1,6-glucan moiety can be linked to b-1,3-glucan or chitin, the cell wall GPI-modified proteins are strongly linked to the cell wall Klis et al, 2001;Richard & Plaine, 2007).GPI-modified proteins share a similar structure: an Nterminal sequence for translocation into the endoplasmic reticulum, a mature domain, and a C-terminal hydrophobic region for anchorage to the endoplasmic reticulum membrane. Nine or ten amino acids before this C-terminal sequence the so-called v site is localized, where the protein is cleaved prior to its ligation to a pre-assembled GPI anchor (Thomas et al, 1990).…”

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confidence: 99%

“…There are 115 putative GPI-modified proteins in C. albicans and most of them have unknown functions. However, several have been implicated in processes such as cell wall biogenesis and remodelling, oxidant adaptation and adherence, or have specific enzymic functions (reviewed by Richard & Plaine, 2007).In a previous study we have shown that the C. albicans PGA59 and PGA62 genes, encoding two related cell wall GPI-modified proteins, are expressed to much higher levels in biofilms than in planktonic cultures (Garcia-Sanchez et al, 2004). The ability of C. albicans to form biofilmsthree-dimensional microbial communities attached to a surface and embedded in an extracellular matrix -plays important roles in the virulence of this fungus and in the management of C. albicans infections, since biofilm cells show decreased susceptibility to most antifungals.…”

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The GPI-modified proteins Pga59 and Pga62 of Candida albicans are required for cell wall integrity

et al. 2009

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The fungal cell wall is essential in maintaining cellular integrity and plays key roles in the interplay between fungal pathogens and their hosts. The PGA59 and PGA62 genes encode two short and related glycosylphosphatidylinositol-anchored cell wall proteins and their expression has been previously shown to be strongly upregulated when the human pathogen Candida albicans grows as biofilms. Using GFP fusion proteins, we have shown that Pga59 and Pga62 are cell-walllocated, N-and O-glycosylated proteins. The characterization of C. albicans pga59D/pga59D, pga62D/pga62D and pga59D/pga59D pga62D/pga62D mutants suggested a minor role of these two proteins in hyphal morphogenesis and that they are not critical to biofilm formation. Importantly, the sensitivity to different cell-wall-perturbing agents was altered in these mutants. In particular, simultaneous inactivation of PGA59 and PGA62 resulted in high sensitivity to Calcofluor white, Congo red and nikkomicin Z and in resistance to caspofungin. Furthermore, cell wall composition and observation by transmission electron microscopy indicated an altered cell wall structure in the mutant strains. Collectively, these data suggest that the cell wall proteins Pga59 and Pga62 contribute to cell wall stability and structure. INTRODUCTIONThe cell wall is an essential component of fungal cells, preserving cellular integrity and playing a central role in the interaction of fungi with their environment. This is particularly the case for pathogenic fungi such as the opportunistic yeast pathogen Candida albicans, where the cell wall has been shown to play central roles in adhesion, virulence, biofilm formation, infection and immunomodulation (Albrecht et al., 2006;Douglas, 2003;Netea et al., 2006;Richard et al., 2002b;Sundstrom, 2002). Because of the essential role of the cell wall in cellular integrity and fungal specificity of some enzymes involved in its biogenesis, it is a recognized target for the development of novel antifungals (e.g. echinocandins that target the b-1,3-glucan synthase) (Latge, 2007).The organization of the fungal cell wall has been mainly characterized in the yeasts Saccharomyces cerevisiae and C. albicans and in the filamentous fungus Aspergillus fumigatus (Klis et al., 2006;Latge, 2007;Lesage & Bussey, 2006;Ruiz-Herrera et al., 2006). The yeast cell wall has a bilayered structure. The inner part is composed of a network of b-1,3-glucan molecules linked by hydrogen bonds. These chains can be bound covalently to b-1,6-glucan molecules and to chitin chains. The outer part of the cell wall is composed mainly of mannoproteins (Klis et al., 2006Lesage & Bussey, 2006). Most proteins in the cell wall of ascomycetous yeasts are glycosylphosphatidylinositolanchored proteins (GPI-modified proteins) that become covalently linked to b-1,6-glucan through a remnant of their GPI anchor. As the b-1,6-glucan moiety can be linked to b-1,3-glucan or chitin, the cell wall GPI-modified proteins are strongly linked to the cell wall Klis et al., 2001;Richard & Plaine, 2007).GPI-...

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Section: Pga59 and Pga62 Are Cell Wall Proteinsmentioning

confidence: 99%

mentioning

confidence: 99%

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The GPI-modified proteins Pga59 and Pga62 of Candida albicans are required for cell wall integrity

et al. 2009

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“…In Candida albicans, GPI-anchored proteins have been identified that are involved in adhesion (the ALS family of proteins and Hwp1), in cell wall biogenesis (Ecm33p) and in protection against host defences (SOD) (Richard & Plaine, 2007). Not surprisingly, therefore, disruptions in these genes, for example in Ecm33p, have been shown to cause reduced virulence (Martinez-Lopez et al, 2004, 2006.…”

Section: Introductionmentioning

confidence: 99%

The Candida albicans homologue of PIG-P, CaGpi19p: gene dosage and role in growth and filamentation

2010

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Glycosylphosphatidyl inositol (GPI)-anchored proteins in Candida albicans are responsible for a vast range of functions, and deletions in certain GPI-anchored proteins severely reduce adhesion and virulence of this organism. In addition, completely modified GPIs are necessary for virulence. GPI anchor biosynthesis is essential for viability and starts with the transfer of N-acetylglucosamine to phosphatidylinositol. This step is catalysed by a multi-subunit complex, GPI–N-acetylglucosaminyltransferase (GPI–GnT). In this, the first report to our knowledge on a subunit of the Candida GPI–GnT complex, we show that CaGpi19p is the functional equivalent of the Saccharomyces cerevisiae Gpi19p. An N-terminal truncation mutant of CaGpi19p functionally complements a conditionally lethal S. cerevisiae gpi19 mutant. Further, we constructed a conditional null mutant of CaGPI19 by disrupting one allele and placing the remaining copy under the control of the MET3 promoter. Repression leads to growth defects, cell wall biogenesis aberrations, azole sensitivity and hyperfilamention. In addition, there is a noticeable gene dosage effect, with the heterozygote also displaying intermediate degrees of most phenotypes. The mutants also displayed a reduced susceptibility to the antifungal agent amphotericin B. Collectively, the results suggest that CaGPI19 is required for normal morphology and cell wall architecture.

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“…2C). C. albicans is thought to possess twice the number of GPI-anchored proteins of S. cerevisiae (Richard & Plaine, 2007). GPI anchors are essentially identical to those of other eukaryotes, and their biosynthesis follows the same pathway.…”

Section: (C) Yeast and Fungal Mannosidesmentioning

confidence: 99%

Mannoside recognition and degradation by bacteria

et al. 2016

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Mannosides constitute a vast group of glycans widely distributed in nature. Produced by almost all organisms, these carbohydrates are involved in numerous cellular processes, such as cell structuration, protein maturation and signalling, mediation of protein-protein interactions and cell recognition. The ubiquitous presence of mannosides in the environment means they are a reliable source of carbon and energy for bacteria, which have developed complex strategies to harvest them. This review focuses on the various mannosides that can be found in nature and details their structure. It underlines their involvement in cellular interactions and finally describes the latest discoveries regarding the catalytic machinery and metabolic pathways that bacteria have developed to metabolize them.

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Comprehensive Analysis of Glycosylphosphatidylinositol-Anchored Proteins in Candida albicans

Cited by 143 publications

References 65 publications

The GPI-modified proteins Pga59 and Pga62 of Candida albicans are required for cell wall integrity

The GPI-modified proteins Pga59 and Pga62 of Candida albicans are required for cell wall integrity

The Candida albicans homologue of PIG-P, CaGpi19p: gene dosage and role in growth and filamentation

Mannoside recognition and degradation by bacteria

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