The influence of Congo red on the cell wall and (1 → 3)-β-d-glucan microfibril biogenesis in Saccharomyces cerevisiae

Kopecká, Marie; Gabriel, Miroslav

doi:10.1007/bf00245214

Cited by 141 publications

(118 citation statements)

References 35 publications

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“…Inhibition of glucan synthesis in vivo and in vitro and cell-wide localization and direct binding of purified glucan indicate that the compound can bind to β-1,3-glucans in the growing glucan fibrils as well as the mature wall. The cell wall dye Congo red may also bind growing glucan fibrils (48), but it also binds to chitin, and biochemical evidence indicates that the primary target of Congo red is chitin (49). Poacic acid targets the β-1,3-glucan layer of fungal cell walls in a manner distinct from that of other cell wall-affecting agents (e.g., caspofungin and nikkomycin Z) and therefore, represents a previously undescribed compound targeting β-1,3-glucan.…”

Section: Discussionmentioning

confidence: 99%

Plant-derived antifungal agent poacic acid targets β-1,3-glucan

Piotrowski

Okada

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

136

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A rise in resistance to current antifungals necessitates strategies to identify alternative sources of effective fungicides. We report the discovery of poacic acid, a potent antifungal compound found in lignocellulosic hydrolysates of grasses. Chemical genomics using Saccharomyces cerevisiae showed that loss of cell wall synthesis and maintenance genes conferred increased sensitivity to poacic acid. Morphological analysis revealed that cells treated with poacic acid behaved similarly to cells treated with other cell wall-targeting drugs and mutants with deletions in genes involved in processes related to cell wall biogenesis. Poacic acid causes rapid cell lysis and is synergistic with caspofungin and fluconazole. The cellular target was identified; poacic acid localized to the cell wall and inhibited β-1,3-glucan synthesis in vivo and in vitro, apparently by directly binding β-1,3-glucan. Through its activity on the glucan layer, poacic acid inhibits growth of the fungi Sclerotinia sclerotiorum and Alternaria solani as well as the oomycete Phytophthora sojae. A single application of poacic acid to leaves infected with the broad-range fungal pathogen S. sclerotiorum substantially reduced lesion development. The discovery of poacic acid as a natural antifungal agent targeting β-1,3-glucan highlights the potential side use of products generated in the processing of renewable biomass toward biofuels as a source of valuable bioactive compounds and further clarifies the nature and mechanism of fermentation inhibitors found in lignocellulosic hydrolysates.

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Section: Discussionmentioning

confidence: 99%

Plant-derived antifungal agent poacic acid targets β-1,3-glucan

Piotrowski

Okada

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

136

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“…All of these cause spherical cell swelling and lysis. The dyes Calcofluor and Congo Red, which inhibit chitin maturation and crystallization (Kopecka and Gabriel, 1992;Bartnicki-Garcia et al, 1994;Engle et al, 1994), similarly cause cell tip swelling, spherical growth, a thickened cell wall, and lysis (Pancaldi et al, 1984;Roncero and Duran, 1985;Dawe and Morris, unpublished data). Actin colocalizes with the site of new cell wall deposition at the growing hyphal tip in filamentous fungi and at the bud tip in yeast.…”

Section: Discussionmentioning

confidence: 99%

Deletion of nudC, a nuclear migration gene of Aspergillus nidulans, causes morphological and cell wall abnormalities and is lethal.

Chiu¹,

Xiang²,

Dawe³

et al. 1997

MBoC

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Nuclear migration is required for normal development in both higher and lower eukaryotes. In fungi this process is mediated by cytoplasmic dynein. It is believed that this motor protein is anchored to the cell membrane and moves nuclei by capturing and pulling on spindle pole body microtubules. To date, four genes have been identified and shown to be required for this process in Aspergillus nidulans. The nudA and nudG genes, respectively, encode the heavy and light chains of cytoplasmic dynein, and the nudF and nudC gene products encode proteins of 49 and 22 kDa. The precise biochemical functions of the nudF and nudC genes have not yet been identified. In this report we further investigate NUDC protein function by deleting the nudC gene. Surprisingly, although deletion of nudA and nudF affect nuclear migration, deletion of nudC profoundly affected the morphology and composition of the cell wall. Spores of the strain deleted for nudC grew spherically and lysed. The thickness of the cell wall was increased in the deletion mutant and wall polymer composition was abnormal. This phenotype could be repressed by growth on osmotically buffered medium at low temperature. Similar, but less severe, effects were also noted in a strain depleted for NUDC by down-regulation. These results suggest a possible relationship between fungal cell wall biosynthesis and nuclear migration.

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“…Both the null mutant and the overexpressing strain behaved similarly to the parental strain with respect to growth rates, morphology and kinetics of germ tube formation, indicating that CaSsr1p is not absolutely necessary for viability in cells growing under the experimental conditions and for the dimorphic transition. CW and CR are compounds that interfere with the assembly of polymers in the cell wall (Elorza et al, 1983;Kopecka & Gabriel, 1992) and they have been used for detecting S. cerevisiae cell-wall mutants (Ram et al, 1994;van der Vaart et al, 1995); when both the Cassr1D null mutant and an overexpressing strain were grown in media containing either CW or CR, an increased sensitivity was observed when compared to the parental strain. This result suggests that in a normal cell-wall structure CaSsr1p must be present in an adequate concentration with respect to the other cell-wall components, and that any deviation from this concentration causes a change in the architecture of that structure as in S. cerevisiae (Moukadiri et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein

et al. 2003

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After screening of a Candida albicans genome database, the product of an ORF (IPF 3054) that has 62 % homology with Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-b-glucanase) and therefore seems to be covalently linked to the b-glucan of the cell walls. Both disruption and overexpression of the CaSSR1 gene caused an increased sensitivity to calcofluor white, Congo red and zymolyase digestion. These results suggest that CaSsr1p has a structural role associated with the cell-wall b-glucan. INTRODUCTIONCandida albicans is an opportunistic pathogenic fungus in humans which can cause either septicaemic or mucosal infections (Odds, 1988(Odds, , 1994. The number of fungal infections caused by C. albicans has increased dramatically in the last few decades, due to the rise in the number of immunocompromised patients and their life expectancies (Fox, 1993). C. albicans is a dimorphic organism capable of reproducing by budding (yeast cells) or by producing germ tubes (mycelial cells) depending upon environmental factors (Odds, 1988); this morphological transition has been associated with pathogenicity (Calderone & Braun, 1991;Odds, 1988;Sentandreu et al., 1993). Because the cell wall of C. albicans is the fungal structure responsible for the initial interaction with the host and for the characteristic shape of each growth form, several studies have focused on its biosynthesis and function (Gozalbo et al., 1994;Sentandreu et al., 1993;Valentin et al., 2000).The cell wall of C. albicans is a complex biochemical entity composed mainly of three components, namely, glucans (1,3-b-and 1,6-b-glucan), mannoproteins and chitin (Fleet, 1991;Valentin et al., 2000). The b-glucans are the main components, accounting for 50-60 % by weight of the cell wall in C. albicans and other fungi. Chitin, a linear polymer of 1,4-b-linked N-acetylglucosamine units, is a relatively minor (1-10 %) but important constituent. In most fungi, b-glucans and chitin polymers account for the rigidity of the cell wall as well as its morphology . Mannoproteins represent 30-40 % of the total cell wall and determine the surface properties, enabling C. albicans cells to interact and adhere to host tissues (Chaffin et al., 1998).Cell-wall mannoproteins can be divided into three groups according to the methods used for their extraction. One group can be solubilized by detergents, such as SDS, or chaotropic agents, such as urea, and is formed by mannoproteins loosely associated with other components of the cell wall (Elorza et al., 1985;Valentin et al., 1984). The second group can be extracted by reducing agents, DTT or b-mercaptoethanol (Casanova et al., 1989;Orlean et al., 1986). The third group can be released from the ce...

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The influence of Congo red on the cell wall and (1 → 3)-β-d-glucan microfibril biogenesis in Saccharomyces cerevisiae

Cited by 141 publications

References 35 publications

Plant-derived antifungal agent poacic acid targets β-1,3-glucan

Plant-derived antifungal agent poacic acid targets β-1,3-glucan

Deletion of nudC, a nuclear migration gene of Aspergillus nidulans, causes morphological and cell wall abnormalities and is lethal.

Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein

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