Critical steps in fungal cell wall synthesis: Strategies for their inhibition

Gozalbo, Daniel; Elorza, M. Victoria; Sanjuan, Raquel; Marcilla, Antonio; Valentı́n, Eulogio; Sentandreu, Rafael

doi:10.1016/0163-7258(93)90015-6

Cited by 30 publications

(22 citation statements)

References 20 publications

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“…A different topological location of the protein in the cell wall may account for the lack of correlation between IIF and GAPDH activity, and it is in accordance with the contention that changes in the cell wall organization occur during the morphogenetic transition (10,19,47); taking into account that GAPDH is a surface antigen, as FIG. 5.…”

Section: Resultssupporting

confidence: 56%

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

et al. 1997

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A gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and their amino acid sequences showed 76% identity; thus, this gene has been named C. albicans TDH1. A rabbit polyclonal antiserum against the purified cytosolic C. albicans GAPDH (polyclonal antibody [PAb] anti-CA-GAPDH) was used to identify the GAPDH in the ␤-mercaptoethanol extracts containing cell wall moieties. Indirect immunofluorescence demonstrated the presence of GAPDH at the C. albicans cell surface, particularly on the blastoconidia. Semiquantitative flow cytometry analysis showed the sensitivity of this GAPDH form to trypsin and its resistance to be removed with 2 M NaCl or 2% sodium dodecyl sulfate. The decrease in fluorescence in the presence of soluble GAPDH indicates the specificity of the labelling. In addition, a dose-dependent GAPDH enzymatic activity was detected in intact blastoconidia and germ tube cells. This activity was reduced by pretreatment of the cells with trypsin, formaldehyde, and PAb anti-CA-GAPDH. These observations indicate that an immunogenic, enzymatically active cell wall-associated form of the glycolytic enzyme GAPDH is found at the cell surface of C. albicans cells.

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Section: Resultssupporting

confidence: 56%

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

et al. 1997

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“…The fungal cell wall is composed of a number of proteins and polysaccharide polymers. Since the wall is essential for viability and is composed of polymers not found in mammals and plants, cell wall biosynthesis is an excellent target for the development of selective antifungal agents (Gozalbo et al, 1993). In Saccharomyces cerevisiae, the cell wall is formed from three principal components: chitin, a…”

Section: Introductionmentioning

confidence: 99%

Multiple Copies ofPBS2,MHP1 orLRE1 Produce Glucanase Resistance and Other Cell Wall Effects inSaccharomyces cerevisiae

Lai¹,

Silverman²,

Gaughran³

et al. 1997

Yeast

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Five sequences were isolated by selection for multiple copy plasmids that conferred resistance to laminarinase, an enzyme that specifically degrades cell wall (1-3) glucan linkages. Strains carrying three of these plasmids showed alterations in cell wall glucan labelling. One of these plasmids carried PBS2, a previously identified, non-essential gene which produces a variety of phenotypes and encodes a mitogen-activated protein kinase kinase analogue (Boguslawski and Polazzi, 1987). Cells carrying PBS2 at multiple copy show a small decrease in cell wall (1-6) glucans. Measurements of (1-3) glucan synthase activity in multi-copy PBS2 cells showed an approximate 30-45% increase in enzyme specific activity while a pbs2 disruption strain showed a decrease in glucan synthase activity of approximately 45% relative to control. A pbs2 disruption strain was laminarinase super-sensitive and supersensitive to K 1 killer toxin while a strain carrying PBS2 at multiple copy was resistant to killer toxin. A second plasmid carried a portion of the MHP1 gene which has been reported to encode a microtubule-interacting protein (Irminger-Finger et al., 1996). The MHP1 gene product is a predicted 1398 amino acid protein and only approximately 80% of the amino portion of this protein is required for laminarinase resistance. Cells carrying the amino portion of MHP1 at multiple copy show a decrease in high molecular weight cell wall (1-6) glucans and were killer toxin resistant while a disruption strain was viable and killer toxin super-sensitive. Cells carrying this plasmid showed decreased levels of high molecular weight (1-6) glucans and increased glucan synthase activity. The laminarinase resistance conferred by the third plasmid mapped to the previously uncharacterized YCL051W open reading frame and this gene was therefore named LRE1 (laminarinase resistance). The LRE1 gene encodes a non-essential 604 amino acid hydrophilic protein. Unexpectedly, cells carrying LRE1 at multiple copy show no alteration in cell wall glucans or glucan synthase activity. Subcloning experiments demonstrated that the production of these cell wall effects requires the presence of both LRE1 and YCL052C (PBN1), a second open reading frame present on the original plasmid. Cells carrying multiple copies of PBN1 alone show no significant alterations in cell wall glucans or glucan synthase activity, indicating that these effects require the presence of multiple copies of both genes.

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“…Several cyclic peptides can impair biosynthesis of macromolecular components of the microbial cell wall such as glucan, chitin, and mannoproteins (Debono and Gordee, 1994). The microbial cell wall is a selective target for antimicrobial agents, excluding target-related deleterious effects on host cells (Georgopapadakou and Tkacz, 1995; Gooday, 1977; Gozalbo et al, 1993). …”

Section: Natural Cyclic Peptides As a Disruptor Of Structural Integrimentioning

confidence: 99%

Antimicrobial Cyclic Peptides for Plant Disease Control

Lee

Kim

2015

The Plant Pathology Journal

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Antimicrobial cyclic peptides derived from microbes bind stably with target sites, have a tolerance to hydrolysis by proteases, and a favorable degradability under field conditions, which make them an attractive proposition for use as agricultural fungicides. Antimicrobial cyclic peptides are classified according to the types of bonds within the ring structure; homodetic, heterodetic, and complex cyclic peptides, which in turn reflect diverse physicochemical features. Most antimicrobial cyclic peptides affect the integrity of the cell envelope. This is achieved through direct interaction with the cell membrane or disturbance of the cell wall and membrane component biosynthesis such as chitin, glucan, and sphingolipid. These are specific and selective targets providing reliable activity and safety for non-target organisms. Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses. Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

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Critical steps in fungal cell wall synthesis: Strategies for their inhibition

Cited by 30 publications

References 20 publications

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

Multiple Copies ofPBS2,MHP1 orLRE1 Produce Glucanase Resistance and Other Cell Wall Effects inSaccharomyces cerevisiae

Antimicrobial Cyclic Peptides for Plant Disease Control

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