Amphotericin B Resistance and Membrane Fluidity in Kluyveromyces lactis Strains
AUTOR(ES)
Younsi, Mohamed
FONTE
American Society for Microbiology
RESUMO
The membrane fluidity of reduced-amphotericin B (AmB)-sensitivity Kluyveromyces lactis mutant strain is higher than that of the wild-type K. lactis strain. After culture of the K. lactis and K. lactis mutant cells in the presence of subinhibitory doses of AmB (10 and 125 mg/liter, respectively), the plasma membranes of both yeast strains also showed a higher fluidity than did those of control cells. High membrane fluidity was associated with changes in the structural properties of the membranes. Culture of the K. lactis and K. lactis mutant cells in the presence of AmB induced changes in membrane lipid contents. In particular, phospholipid contents were increased in both strains treated with AmB, compared with their corresponding counterparts. As a result, the sterol/phospholipid ratio decreased. The relative proportion of monounsaturated fatty acids also increased after AmB treatment. The saturated fatty acid/monounsaturated fatty acid ratio decreased in K. lactis and K. lactis mutant cells treated with AmB but also in K. lactis mutant control cells compared to that in the K. lactis wild strain. These changes in lipid composition explain the higher fluidity, which could represent a process of metabolic resistance of the yeasts to AmB.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=89984Documentos Relacionados
- Miconazole and amphotericin B alter polymorphonuclear leukocyte functions and membrane fluidity in similar fashions.
- Obtaining of recombinant strains of the yeast Kluyveromyces lactis producers of streptavidin
- Toxicity and induction of resistance to Listeria monocytogenes infection by amphotericin B in inbred strains of mice.
- Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
- Efficient Homolactic Fermentation by Kluyveromyces lactis Strains Defective in Pyruvate Utilization and Transformed with the Heterologous LDH Gene†