Cell Wall-Related Bionumbers and Bioestimates of Saccharomyces cerevisiae and Candida albicans

Klis, Frans M.; Koster, Chris G. de; Brul, Stanley

doi:10.1128/ec.00250-13

Cited by 93 publications

(76 citation statements)

References 88 publications

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“…At the same time, it was also demonstrated that cell wall structure and physical properties can vary depending on temperature, pH, as well as growth conditions and phase (29). At the end of late-exponential stage and by the entering stationary phase, cell wall becomes thicker, more resistant to various agents, and less permeable to macromolecules (30).…”

Section: Discussionmentioning

confidence: 99%

“…It was previously estimated that the total number of ␤-1,6-glucan molecules in a haploid parent cell of S. cerevisiae at exponential growth phase is 6.6 ϫ 10 6 (29). At the same time, it was also demonstrated that cell wall structure and physical properties can vary depending on temperature, pH, as well as growth conditions and phase (29).…”

Section: Discussionmentioning

confidence: 99%

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Yeast β-1,6-Glucan Is a Primary Target for the Saccharomyces cerevisiae K2 Toxin

et al. 2015

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b Certain Saccharomyces cerevisiae strains secrete different killer proteins of double-stranded-RNA origin. These proteins confer a growth advantage to their host by increasing its survival. K2 toxin affects the target cell by binding to the cell surface, disrupting the plasma membrane integrity, and inducing ion leakage. In this study, we determined that K2 toxin saturates the yeast cell surface receptors in 10 min. The apparent amount of K2 toxin, bound to a single cell of wild type yeast under saturating conditions, was estimated to be 435 to 460 molecules. It was found that an increased level of ␤-1,6-glucan directly correlates with the number of toxin molecules bound, thereby impacting the morphology and determining the fate of the yeast cell. We observed that the binding of K2 toxin to the yeast surface receptors proceeds in a similar manner as in case of the related K1 killer protein. It was demonstrated that the externally supplied pustulan, a poly-␤-1,6-glucan, but not the glucans bearing other linkage types (such as laminarin, chitin, and pullulan) efficiently inhibits the K2 toxin killing activity. In addition, the analysis of toxin binding to the intact cells and spheroplasts confirmed that majority of K2 protein molecules attach to the ␤-1,6-glucan, rather than the plasma membrane-localized receptors. Taken together, our results reveal that ␤-1,6-glucan is a primary target of K2 toxin and is important for the execution of its killing property.T he production of antimycotic killer toxins has been observed in several yeast genera and proved to be a widespread phenomenon (1, 2). Killer strains of Saccharomyces cerevisiae secrete protein toxins derived from a family of double-stranded RNAs (dsRNAs). The toxins have been grouped into four types (K1, K2, K28, and Klus) based on their killing profiles and lack of crossimmunity (3, 4). Such proteins are able to kill the nonkiller yeast, as well as yeast of other killer types, while the toxin-producing cells remain immune to their own or to the same type of killers (4, 5). K1 toxin disrupts the regulated ion flux across the plasma membrane, leading to the death of sensitive yeast strains (6, 7). The killing action of K1 toxin involves at least two steps. During the first step, the toxin binds to the cell wall, whereas the second step leads to the translocation and insertion of the toxin into the plasma membrane (6). Beta-1,6-glucan was originally proposed to be a cell wall receptor for K1 (8). Analysis of several kre mutants demonstrated that decrease of the cell wall ␤-1,6-glucan level leads to K1 resistance, thus confirming the involvement of this type of glucan in toxin binding (9). During the second step, K1 toxin interacts with plasma membrane receptors and disrupts the functional integrity of the plasma membrane either by inducing the formation of new ion channels (7) or through the activation of existing potassium channels (10). Products of TOK1 (protein, forming the potassium ion channel) and KRE1 (glycoprotein, involved in ␤-glucan assembly) have be...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Yeast β-1,6-Glucan Is a Primary Target for the Saccharomyces cerevisiae K2 Toxin

et al. 2015

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“…Theoretically, about 90 GS molecules Fkslp should be accumulated in one AP/FLI to produce one b-1,3-glucan microfibril of 10 nm in width. A single GS can synthesize (in cooperation with other enzymes) (Klis 1994;Orlean 2012;Teparić & Mrša, 2013;Klis et al, 2014) only a single branched b-1,3-glucan molecule of an amorphous glucan matrix along the cell surface. However, we have no evidence to confirm this, because the cell wall layer of the mother cells remained unchanged after LA treatment; the cells only became spherical and larger.…”

Section: Discussionmentioning

confidence: 99%

“…Our reinvestigation of the phenotypes of act1-1 and act1-2 mutant cells at 37 uC proved that AC are necessary for the correct spatial positioning and orientation of secretory pathways to the bud and septum, and for vectorial movement of the SV along the AC ; act1-1 cells at 23 uC have 'faint actin cables' that delay bud formation, bud growth and nuclear migration to the bud neck, in contrast to nuclear division Kopecká & Yamaguchi, 2011). This indicated the existence of two cytoskeleton-dependent pathways: (i) the 'actin pathway' for bud formation, bud growth and nuclear migration, and (ii) the 'microtubule pathway' for nuclear division (Kopecká & Yamaguchi, 2011) that may correspond to the two cell-cycle pathways identified by CDC mutants (Hartwell et al, 1974 Klis et al, 2014) that under examination with electron microscopy have an amorphous appearance (Kopecká et al, 1974).…”

Section: Introductionmentioning

confidence: 99%

Effects of the F-actin inhibitor latrunculin A on the budding yeast Saccharomyces cerevisiae

2015

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Our basic cell biology research was aimed at investigating the effect on eukaryotic cells of the sudden loss of the F-actin cytoskeleton. Cells treated with latrunculin A (LA) in yeast extract peptone dextrose (YEPD) medium were examined using phase-contrast and fluorescent microscopy, freeze-substitution, transmission and scanning electron microscopy, counted using a Bü rker chamber and their absorbance measured. The cells responded to the presence of LA, an F-actin inhibitor, with the disappearance of actin patches, actin cables and actin rings. This resulted in the formation of larger spherical cells with irregular morphology in the cell walls and ultrastructural disorder of the cell organelles and secretory vesicles. Instead of buds, LA-inhibited cells formed only 'table-mountain-like' wide flattened swellings without apical growth with a thinner glucan cell-wall layer containing b-1,3-glucan microfibrils. The LA-inhibited cells lysed. Actin cables and patches were required for bud formation and bud growth. In addition, actin patches were required for the formation of b-1,3-glucan microfibrils in the bud cell wall. LA has fungistatic, fungicidal and fungilytic effects on the budding yeast Saccharomyces cerevisiae.

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“…This type of yeast was selected due to the fact that it represents a cell biomass of the top fermenting yeast and is composed of living cells capable of producing fermentation of sugars without requiring a culture medium. These cells absorb the easiest hexoses (glucose) and then sucrose and maltose [43][44][45][46][47]. Glucose monohydrate was supplied by S.C. Chemical Company S.A., Ias,i, Romania.…”

Section: Methodsmentioning

confidence: 99%

Microencapsulation of Baker’s Yeast in Gellan Gum Beads Used in Repeated Cycles of Glucose Fermentation

Iurciuc

Peptu

Savin

et al. 2017

International Journal of Polymer Science

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The purpose of this work is to prepare ionically cross-linked (with CaCl 2 ) gellan particles with immobilized yeast cells for their use in repeated fermentation cycles of glucose. The study investigates the influence of ionic cross-linker concentration on the stability and physical properties of the particles obtained before extrusion and during time in the coagulation bath (the cross-linker solution with different CaCl 2 concentrations). It was found that by increasing the amount of the cross-linker the degree of cross-linking in the spherical gellan matrix increases, having a direct influence on the particle morphology and swelling degree in water. These characteristics were found to be very important for diffusion of substrate, that is, the glucose, into the yeast immobilized cells and for the biocatalytic activity of the yeast immobilized cells in gellan particles. These results highlight the potential of these bioreactors to be used in repeated fermentation cycles (minimum 10) without reducing their biocatalytic activity and maintaining their productivity at similar parameters to those obtained in the free yeast fermentation. Encapsulation of Saccharomyces cerevisiae into the gellan gum beads plays a role in the effective application of immobilized yeast for the fermentation process.

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Cell Wall-Related Bionumbers and Bioestimates of Saccharomyces cerevisiae and Candida albicans

Cited by 93 publications

References 88 publications

Yeast β-1,6-Glucan Is a Primary Target for the Saccharomyces cerevisiae K2 Toxin

Yeast β-1,6-Glucan Is a Primary Target for the Saccharomyces cerevisiae K2 Toxin

Effects of the F-actin inhibitor latrunculin A on the budding yeast Saccharomyces cerevisiae

Microencapsulation of Baker’s Yeast in Gellan Gum Beads Used in Repeated Cycles of Glucose Fermentation

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