دورية أكاديمية
Involvement of [beta]-glucans in the wide-spectrum antimicrobial activity of Williopsis saturnus var. mrakii MUCL 41968 killer toxin.
| العنوان: | Involvement of [beta]-glucans in the wide-spectrum antimicrobial activity of Williopsis saturnus var. mrakii MUCL 41968 killer toxin. |
|---|---|
| المؤلفون: | Guyard C, Dehecq E, Tissier JP, Polonelli L, Dei-Cas E, Cailliez JC, Menozzi FD |
| المصدر: | Molecular medicine (Cambridge, Mass.) [Mol Med] 2002 Nov; Vol. 8 (11), pp. 686-94. |
| نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: BioMed Central Country of Publication: England NLM ID: 9501023 Publication Model: Print Cited Medium: Print ISSN: 1076-1551 (Print) Linking ISSN: 10761551 NLM ISO Abbreviation: Mol Med Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2018- : [London, United Kingdom] : BioMed Central Original Publication: Cambridge, Mass. : Blackwell Scientific Publications, c1994- |
| مواضيع طبية MeSH: | Anti-Infective Agents/*pharmacology , Fungal Proteins/*pharmacology , Glucans/*metabolism , Mycotoxins/*pharmacology , Saccharomyces cerevisiae/*drug effects , Spheroplasts/*drug effects, Amphotericin B/pharmacology ; Anti-Bacterial Agents ; Antifungal Agents/pharmacology ; Cell Death ; Colony Count, Microbial ; Drug Resistance, Microbial ; Enzyme Inhibitors/pharmacology ; Flow Cytometry ; Hydrolases/pharmacology ; Indolizines/pharmacology ; Killer Factors, Yeast ; Nitrophenols/metabolism ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins ; beta-Glucosidase/antagonists & inhibitors ; beta-Glucosidase/metabolism |
| مستخلص: | Background: Williopsis saturnus var. mrakii MUCL 41968 secretes a 85-kDa glycoprotein killer toxin (WmKT) that displays a cytocidal activity against a wide range of microorganisms, making WmKT a promising candidate for the development of new antimicrobial molecules. Although the killing mechanism of WmKT is still unknown, the toxin was recently proposed to bind to the surface of sensitive microorganisms through the recognition of beta-glucans. Indeed, Saccharomyces cerevisiae strains sensitive to the toxin become resistant when mutated in their beta-glucan synthesis pathway. Materials and Methods: To investigate the interaction of WmKT with beta-glucans, we examined in agar diffusion assays the WmKT activity in the presence of enzymes displaying beta-glucanase activity. The toxin activity was also investigated using spheroplasts derived from sensitive yeast cells. The hydrolytic activity of WmKT was studied using specific glucosidase inhibitors as well as various sugar molecules covalently linked to p-nitrophenyl as potential substrates. Finally, the ultrastructural modifications induced by WmKT activity on sensitive yeasts were assessed by scanning electron microscopy. Results: The data reported here support the hypothesis that WmKT binds to sensitive cells using surface-exposed beta-glucans. Indeed beta-glucanase exerts an antagonistic effect on WmKT activity and spheroplasts derived from WmKT-sensitive yeast cells are shown to be resistant to WmKT, suggesting that cell wall beta-glucans are required for WmKT lethal effect. Because WmKT exhibits amino acid sequence similarities with proteins suspected to be glucanase, we also investigated the effect of castanospermine, a potent glucosidase inhibitor, on WmKT activity. Castanospermine completely abolished WmKT killer activity as well as its hydrolytic enzymatic activity against p-nitrophenyl beta-D-glucopyranoside. The scanning electron microscopy analysis of sensitive yeast cells treated with the toxin reveals that WmKT causes cell wall modifications similar to those observed with zymolyase. Conclusion: The results reported in this study show that WmKT activity requires an interaction between the mycocin and the cell wall beta-glucans. Moreover, they indicate that WmKT acts on sensitive yeast cells through a hydrolytic activity directed against cell wall beta-glucans that disrupts the yeast cell wall integrity leading to death. |
| المشرفين على المادة: | 0 (Anti-Bacterial Agents) 0 (Anti-Infective Agents) 0 (Antifungal Agents) 0 (Enzyme Inhibitors) 0 (Fungal Proteins) 0 (Glucans) 0 (Indolizines) 0 (Killer Factors, Yeast) 0 (Mycotoxins) 0 (Nitrophenols) 0 (Saccharomyces cerevisiae Proteins) 37340-57-1 (zymolyase) 7XU7A7DROE (Amphotericin B) EC 3.- (Hydrolases) EC 3.2.1.21 (beta-Glucosidase) Q0I3184XM7 (castanospermine) Y92ZL45L4R (4-nitrophenol) |
| تواريخ الأحداث: | Date Created: 20030110 Date Completed: 20030613 Latest Revision: 20180821 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC2039955 |
| PMID: | 12520085 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Springer Verlag. 
Full Text Finder كن أول من يترك تعليقا!