title: 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.
abstract: 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.
authors.affiliation: Unilever Research Vlaardingen, The Netherlands.
authors.forename: I J
authors.initials: IJ
authors.lastname: Bom
authors.forename: F M
authors.initials: FM
authors.lastname: Klis
authors.forename: H
authors.initials: H
authors.lastname: de Nobel
authors.forename: S
authors.initials: S
authors.lastname: Brul
mesh_terms: D000935:Antifungal Agents / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D002462:Cell Membrane / Q000187:drug effects; D002473:Cell Wall / Q000187:drug effects / Q000378:metabolism; D004187:Disaccharides / Q000494:pharmacology; D005516:Food Microbiology; D005936:Glucans / Q000737:chemistry; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D006867:Hydrolases / Q000494:pharmacology; D008565:Membrane Proteins / Q000187:drug effects / Q000378:metabolism; D009844:Oligosaccharides / Q000737:chemistry / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D011134:Polysaccharides / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000254:growth & development; D020068:Zygosaccharomyces / Q000187:drug effects* / Q000254:growth & development; D047071:beta-Glucans
chemical_list: D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D004187:Disaccharides; D005936:Glucans; D017261:Glycosylphosphatidylinositols; C414549:MB21 peptide; D008565:Membrane Proteins; D009844:Oligosaccharides; D010455:Peptides; D011134:Polysaccharides; D047071:beta-Glucans; C002076:pustulan; C037833:zymolyase; C064197:beta-1,6-glucan; D006867:Hydrolases; C100052:gentiobiose