scholarly journals A common mechanism involving the TORC1 pathway can lead to amphotericin B-persistence in biofilm and planktonic Saccharomyces cerevisiae populations

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Rasmus Bojsen ◽  
Birgitte Regenberg ◽  
David Gresham ◽  
Anders Folkesson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amphotericin B ◽  
Common Mechanism

scholarly journals Different polarisome components play distinct roles in Slt2p-regulated cortical ER inheritance in Saccharomyces cerevisiae

2013 ◽  
Vol 24 (19) ◽  
pp. 3145-3154 ◽  
Author(s):  
Xia Li ◽  
Susan Ferro-Novick ◽  
Peter Novick
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Mitogen Activated Protein Kinase ◽  
Common Mechanism ◽  
Late Step ◽  
Mitogen Activated Protein ◽  
Cortical Endoplasmic Reticulum

Ptc1p, a type 2C protein phosphatase, is required for a late step in cortical endoplasmic reticulum (cER) inheritance in Saccharomyces cerevisiae. In ptc1Δ cells, ER tubules migrate from the mother cell and contact the bud tip, yet fail to spread around the bud cortex. This defect results from the failure to inactivate a bud tip–associated pool of the cell wall integrity mitogen-activated protein kinase, Slt2p. Here we report that the polarisome complex affects cER inheritance through its effects on Slt2p, with different components playing distinct roles: Spa2p and Pea2p are required for Slt2p retention at the bud tip, whereas Bni1p, Bud6p, and Sph1p affect the level of Slt2p activation. Depolymerization of actin relieves the ptc1Δ cER inheritance defect, suggesting that in this mutant the ER becomes trapped on the cytoskeleton. Loss of Sec3p also blocks ER inheritance, and, as in ptc1Δ cells, this block is accompanied by activation of Slt2p and is reversed by depolymerization of actin. Our results point to a common mechanism for the regulation of ER inheritance in which Slt2p activity at the bud tip controls the association of the ER with the actin-based cytoskeleton.

scholarly journals In vitro activity of rezafungin against common and rare Candida species and Saccharomyces cerevisiae

2019 ◽  
Vol 74 (12) ◽  
pp. 3505-3510 ◽  
Author(s):  
Zoltán Tóth ◽  
Lajos Forgács ◽  
Jeffrey B Locke ◽  
Gábor Kardos ◽  
Fruzsina Nagy ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amphotericin B ◽  
Candida Species ◽  
Sensu Stricto ◽  
Candida Guilliermondii ◽  
Vitro Activity ◽  
In Vitro Activity ◽  
Candida Auris ◽  
In Vitro Susceptibility

Abstract Background Rezafungin is a novel echinocandin with excellent activity against common Candida species; however, limited data are available regarding rare Candida species. Methods We determined the in vitro susceptibility of 689 clinical isolates of 5 common and 19 rare Candida species, as well as Saccharomyces cerevisiae. The activity of rezafungin was compared with that of anidulafungin, caspofungin, micafungin, amphotericin B and fluconazole, using CLSI broth microdilution methodology (Fourth Edition: M27). Results Rezafungin MIC90 values were 0.06 mg/L for Candida albicans (n=125), Candida tropicalis (n=51), Candida dubliniensis (n=22), Candida inconspicua (n=41), Candida sojae (n=10), Candida lipolytica (n=10) and Candida pulcherrima (n=10), 0.12 mg/L for Candida glabrata (n=81), Candida krusei (n=53), Candida kefyr (n=52) and Candida fabianii (n=15), 0.25 mg/L for Candida lusitaniae (n=46) and Candida auris (n=19), 0.5 mg/L for Candida metapsilosis (n=15) and S. cerevisiae (n=21), 1 mg/L for Candida orthopsilosis (n=15) and Candida guilliermondii (n=27) and 2 mg/L for Candida parapsilosis sensu stricto (n=59). Caspofungin MIC90 values were 0.25–2 mg/L for all species, while micafungin and anidulafungin MIC90 values were similar to those of rezafungin. Fluconazole resistance was found in C. albicans (5.6%) and C. glabrata (4.9%); rezafungin was effective against these isolates as well. Amphotericin B MIC values did not exceed 2 mg/L. Conclusions Rezafungin showed excellent in vitro activity against both WT and azole-resistant Candida species, as well as against S. cerevisiae. Rezafungin had similar activity to other echinocandins (excluding caspofungin) against common Candida species and, notably, against clinically relevant uncommon Candida species.

Visualization analysis of the vacuole-targeting fungicidal activity of amphotericin B against the parent strain and an ergosterol-less mutant of Saccharomyces cerevisiae

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_5) ◽  
pp. 939-947 ◽  
Author(s):  
Chang-Kyung Kang ◽  
Keiichi Yamada ◽  
Yoshinosuke Usuki ◽  
Akira Ogita ◽  
Ken-ichi Fujita ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amphotericin B ◽  
Parent Strain ◽  
Fungicidal Activity ◽  
Visualization Analysis

scholarly journals Bloodstream yeast infections: a 15-month survey

2009 ◽  
Vol 137 (7) ◽  
pp. 1037-1040 ◽  
Author(s):  
D. SWINNE ◽  
N. NOLARD ◽  
P. VAN ROOIJ ◽  
M. DETANDT
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Candida Albicans ◽  
Intensive Care ◽  
Amphotericin B ◽  
Antibacterial Therapy ◽  
Antifungal Agent ◽  
Susceptibility Testing ◽  
Common Species ◽  
Major Surgery ◽  
Predisposing Factor

SUMMARYA 15-month survey of 412 bloodstream yeast isolates from 54 Belgian hospitals was undertaken. Candida albicans was the most common species (47·3%) followed by C. glabrata (25·7%), C. parapsilosis (8·0%), C. tropicalis (6·8%) and Saccharomyces cerevisiae (5·1%). Common predisposing factors were antibacterial therapy (45%), hospitalization in intensive care units (34%), presence of in-dwelling catheters (32%), underlying cancer (23%) and major surgery (11%). Most patients had more than one predisposing factor. Fluconazole alone or in combination with another antifungal agent was the treatment of choice for 86·6% of the cases. Susceptibility testing revealed that 93·5% were susceptible to amphotericin B, 39·6% to itraconazole, 42·8% to fluconazole and 87% to voriconazole. Resistance to azoles was more common among C. glabrata isolates.

scholarly journals Mutations in elongation factor EF-1 alpha affect the frequency of frameshifting and amino acid misincorporation in Saccharomyces cerevisiae.

Genetics ◽  
1988 ◽  
Vol 120 (4) ◽  
pp. 923-934
Author(s):  
M G Sandbaken ◽  
M R Culbertson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Mutational Analysis ◽  
Elongation Factor ◽  
Common Mechanism ◽  
Amino Acid Substitutions ◽  
Protein Amino Acid ◽  
Nonsense Mutations ◽  
Reading Frame

Abstract A mutational analysis of the eukaryotic elongation factor EF-1 alpha indicates that this protein functions to limit the frequency of errors during genetic code translation. We found that both amino acid misincorporation and reading frame errors are controlled by EF-1 alpha. In order to examine the function of this protein, the TEF2 gene, which encodes EF-1 alpha in Saccharomyces cerevisiae, was mutagenized in vitro with hydroxylamine. Sixteen independent TEF2 alleles were isolated by their ability to suppress frameshift mutations. DNA sequence analysis identified eight different sites in the EF-1 alpha protein that elevate the frequency of mistranslation when mutated. These sites are located in two different regions of the protein. Amino acid substitutions located in or near the GTP-binding and hydrolysis domain of the protein cause suppression of frameshift and nonsense mutations. These mutations may effect mistranslation by altering the binding or hydrolysis of GTP. Amino acid substitutions located adjacent to a putative aminoacyl-tRNA binding region also suppress frameshift and nonsense mutations. These mutations may alter the binding of aminoacyl-tRNA by EF-1 alpha. The identification of frameshift and nonsense suppressor mutations in EF-1 alpha indicates a role for this protein in limiting amino acid misincorporation and reading frame errors. We suggest that these types of errors are controlled by a common mechanism or closely related mechanisms.

scholarly journals Comparative studies on cell stimulatory, permeabilizing and toxic effects induced in sensitive and multidrug resistant fungal strains by amphotericin B (AMB) and N-methyl-N-D-fructosyl amphotericin B methyl ester (MFAME).

2000 ◽  
Vol 47 (1) ◽  
pp. 133-140 ◽  
Author(s):  
J Szlinder-Richert ◽  
B Cybulska ◽  
J Grzybowska ◽  
E Borowski ◽  
R Prasad
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Methyl Ester ◽  
Amphotericin B ◽  
Mammalian Cells ◽  
Parent Compound ◽  
Multidrug Resistant ◽  
Solubility In Water ◽  
Good Solubility ◽  
Low Toxicity ◽  
Amphotericin B Methyl Ester

N-Methyl-N-D-fructosyl-amphotericin B methyl ester (MFAME) is a new derivative of amphotericin B, which is characterised by low toxicity to mammalian cells and good solubility in water of its salts. The antifungal activity and effects of MFAME towards Candida albicans and Saccharomyces cerevisiae multidrug resistant MDR(+) and sensitive MDR(-) strains was compared with those of parent compound. The results obtained indicate that MDR(+) S. cerevisiae was sensitive to MFAME as well as to AMB. MFAME exhibited the same effects on fungal cells studied as parent antibiotic. The two antibiotics, depending on the dose applied induced cell stimulation, K+ efflux, and/or had a toxic effect.

Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae

1985 ◽  
Vol 5 (9) ◽  
pp. 2279-2288
Author(s):  
H S Yoo ◽  
F S Genbauffe ◽  
T G Cooper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Gene Cluster ◽  
Common Mechanism ◽  
Physiological Conditions ◽  
Hybridization Probes ◽  
Pathway Gene ◽  
Genes Encoding ◽  
New Gene ◽  
The Right ◽  
Mutant Cells

This report describes the isolation of the genes encoding allantoicase (DAL2) and ureidoglycolate hydrolase (DAL3), which are components of the large DAL gene cluster on the right arm of chromosome IX of Saccharomyces cerevisiae. During this work a new gene (DAL7) was identified and found to be regulated in the manner expected for an allantoin pathway gene. Its expression was (i) induced by allophanate, (ii) sensitive to nitrogen catabolite repression, and (iii) responsive to mutation of the DAL80 and DAL81 loci, which have previously been shown to regulate the allantoin degradation system. Hybridization probes generated from these cloned genes were used to analyze expression of the allantoin pathway genes in wild-type and mutant cells grown under a variety of physiological conditions. When comparison was possible, the patterns of mRNA and enzyme levels observed in various strains and physiological conditions were very similar, suggesting that the system is predominantly regulated at the level of gene expression. Although all of the genes seem to be controlled by a common mechanism, their detailed patterns of expression were, at the same time, highly individual and diverse.

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