A new strategy for inhibition of the spoilage yeasts Saccharomyces cerevisiae and Zygosaccharomyces bailii based on combination of a membrane-active peptide with an oligosaccharide that leads to an impaired glycosylphosphatidylinositol (GPI)-dependent yeast wall protein layer
| Autor: | Stanley Brul, Isaac J. Bom, Hans de Nobel, Frans M. Klis |
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| Rok vydání: | 2003 |
| Předmět: |
Antifungal Agents
beta-Glucans Glycosylphosphatidylinositols Hydrolases Zygosaccharomyces bailii Food spoilage Saccharomyces cerevisiae Oligosaccharides Peptide Zygosaccharomyces Disaccharides Applied Microbiology and Biotechnology Microbiology Cell wall chemistry.chemical_compound Cell Wall Polysaccharides Gentiobiose Glucans chemistry.chemical_classification biology Cell Membrane Membrane Proteins General Medicine biology.organism_classification Yeast chemistry Biochemistry Food Microbiology Peptides Antimicrobial Cationic Peptides |
| Zdroj: | FEMS yeast research. 1(3) |
| ISSN: | 1567-1356 |
| Popis: | Glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in yeast are connected to the beta-1,3-glucan network via a beta-1,6-glucan moiety. Addition of gentiobiose or beta-1,6-glucan oligomers to growing cells affected the construction of a normal layer of GPI-dependent cell wall proteins at the outer rim of the Saccharomyces cerevisiae cell wall. Treated S. cerevisiae cells secreted significant amounts of cell wall protein 2, were much more sensitive to the lytic action of zymolyase 20T and displayed a marked increase in sensitivity to the small amphipathic antimicrobial peptide MB-21. Similar results in terms of sensitization of yeast cells to the antimicrobial peptide were obtained with the notorious food spoilage yeast Zygosaccharomyces bailii. Our results indicate that treating cells with a membrane-perturbing compound together with compounds that lead to an impaired construction of a normal GPI-dependent yeast wall protein layer represents an effective strategy to prevent the growth of major food spoilage yeasts. |
| Databáze: | OpenAIRE |
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