<i>EAP1</i>
            , a
            <i>Candida albicans</i>
            Gene Involved in Binding Human Epithelial Cells

Li, Fang; Palecek, Sean P.

doi:10.1128/ec.2.6.1266-1273.2003

Cited by 168 publications

(161 citation statements)

References 66 publications

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“…1B, D). The 42 aa repeat was shared by other C. albicans cell wall GPI-modified proteins, including the Cht2 chitinase (Dunkler et al, 2005;McCreath et al, 1995), Hwp1 (Staab & Sundstrom, 1998;Sundstrom, 2002), Hwp2 (Sohn et al, 2003), Rbt1 (Braun et al, 2000), Eap1 (Li & Palecek, 2003, Ywp1 (Granger et al, 2005;Sohn et al, 2003), and three putative GPI-modified proteins, Pga6, Pga18 and Pga38. In these proteins the amino acid repeat was 42-46 aa long (Fig.…”

Section: Resultsmentioning

confidence: 99%

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: Resultsmentioning

confidence: 99%

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

et al. 2009

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“…The C. albicans Eap1p adhesin was originally identified because of its ability to mediate adhesion to polystyrene when the EAP1 gene was expressed in a flocculin-deficient Saccharomyces cerevisiae strain. EAP1 expression enhanced attachment of S. cerevisiae to HEK293 kidney epithelial cells and played an additional role in mediating interactions between S. cerevisiae and C. albicans cells (Li & Palecek, 2003, 2005. Expression of EAP1 in a C. albicans efg1/efg1 mutant was able to restore its partially reduced adhesion to HEK293 epithelial cells (Li & Palecek, 2003).…”

Section: Introductionmentioning

confidence: 96%

Distinct domains of the Candida albicans adhesin Eap1p mediate cell–cell and cell–substrate interactions

Palecek

2008

Microbiology

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The adhesion of Candida albicans to host tissues contributes to its virulence, and adhesion to tissues or medical devices is a necessary step in biofilm formation. EAP1 encodes a glycosylphosphatidylinositol (GPI)-anchored glucan-cross-linked cell wall protein that mediates adhesion of C. albicans to various materials and cells, and appears to be required for C. albicans biofilm formation in vitro and in vivo. In this study, we demonstrated that the Eap1p N-terminal signal peptide and C-terminal GPI-anchor sequences result in similar protein localization in Saccharomyces cerevisiae and C. albicans. To investigate the contribution of different Eap1p domains to adhesion, we expressed Eap1p domain deletion mutants in non-adherent S. cerevisiae strains. The N-terminal domain mediates yeast cell-cell adhesion and invasive growth. Two Ser/Thr-rich domains containing tandem repeats were required to project the N-terminal region into the extracellular environment and to mediate adhesion to polystyrene. The N-terminal tandem repeat domain mediated adhesion to mammalian epithelial cells and promoted S. cerevisiae pseudohyphal growth. These results suggest a modular structure of Eap1p in which each domain serves multiple, often distinct, functions.

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“…However, it has some benefits, as it provides quick and efficient method to screen multiple personal care ingredients singly and in combination. Polystyrene has long been used to measure how well bacteria and fungi attach to surfaces [12][13][14][15]. Previous studies have shown that studies on bacteria and fungi with mutations in attachment have also been shown respond to polystyrene and skin surfaces in similar ways [12,15].…”

Section: Discussionmentioning

confidence: 99%

The Effect of Select Personal Care Ingredients and Simple Formulations on the Attachment of Bacteria on Polystyrene

Engelbrecht¹,

Mundschau²,

Chaudhary³

et al. 2018

Cosmetics

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Abstract:The human body is covered with bacteria that are required for health and wellbeing. Additionally, there are pathogenic bacteria that are unwanted. It is therefore important to understand how personal care ingredients interact with these bacteria. To help understand these interactions, a high-throughput assay was developed to study the effect of personal care ingredients on attachment. Seventeen personal care ingredients were assayed singly and in simple alcohol based formulations. Three of the ingredients decreased the attachment of both bacteria tested by 90% singly and in formulation. Personal care ingredients singly and in simple formulations can prevent the attachment of bacteria. Further research is needed to better understand how personal care ingredients affect bacterial attachment and how these effects can be used to create new hygiene products for consumers.

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EAP1 , a Candida albicans Gene Involved in Binding Human Epithelial Cells

Cited by 168 publications

References 66 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

Distinct domains of the Candida albicans adhesin Eap1p mediate cell–cell and cell–substrate interactions

The Effect of Select Personal Care Ingredients and Simple Formulations on the Attachment of Bacteria on Polystyrene

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