Polyene antibiotic affinities for the sterols of resistant and sensitive strains of Neurospora crassa

1977 ◽  
Vol 23 (1) ◽  
pp. 113-115 ◽  
Author(s):  
D. Johnson ◽  
R. Subden
Keyword(s):  
Candida Albicans ◽  
Neurospora Crassa ◽  
Resistant Mutant ◽  
Wild Type ◽  
Polyene Antibiotic ◽  
Polyene Antibiotics ◽  
Mutant Strains ◽  
Resistant Strains

Ergosterol, the principle sterol of many wild-type Neurospora and other Ascomycetes, had a greater affinity for polyene antibiotics than did lichesterol or eburicol, the sterols of some resistant mutant strains. The affinity was demonstrated by comparing the sterols extracted from sensitive and resistant strains of Neurospora crassa and Candida albicans for protection against polyene inhibition of sensitive N. crassa and for their ability to alter specific polyene absorption maxima.

scholarly journals Adenosine kinase-deficient mutant of Neurospora crassa

1982 ◽  
Vol 152 (3) ◽  
pp. 1292-1294
Author(s):  
J M Magill ◽  
P Dalke ◽  
T S Lyda ◽  
C W Magill
Keyword(s):  
Neurospora Crassa ◽  
Resistant Mutant ◽  
Adenosine Kinase ◽  
Deficient Mutant ◽  
Wild Type ◽  
Purine Nucleotides ◽  
Mutant Strains

Tubercidin-resistant mutant strains of Neurospora crassa were isolated, and at least one appeared to be deficient in adenosine kinase. No significant differences in [8-14C]adenosine labeling of purine nucleotides or nucleosides were found between the wild type and the adenosine kinase-deficient strains.

Sterol content and polyene antibiotic resistance in isolates of Candida krusei, Candida parakrusei, and Candida tropicalis

1977 ◽  
Vol 23 (4) ◽  
pp. 398-401 ◽  
Author(s):  
L. M. Safe ◽  
S. H. Safe ◽  
R. E. Subden ◽  
D. C. Morris
Keyword(s):  
Antibiotic Resistance ◽  
Candida Tropicalis ◽  
Candida Krusei ◽  
Sterol Content ◽  
Wild Type ◽  
Polyene Antibiotic ◽  
Polyene Antibiotics ◽  
Resistant Strains

Three isolates, one from each species of Candida krusei, C. parakrusei, and C. tropicalis, obtained from infected patients, were more tolerant of significantly higher concentrations of polyene antibiotics than the corresponding reference wild types. The resistant strains isolated had the same sterols as their wild-type counterparts but in lower concentrations.

Isolation and characterization of Azotobacter vinelandii mutant strains with potential as bacterial fertilizer

1983 ◽  
Vol 29 (8) ◽  
pp. 973-978 ◽  
Author(s):  
Joyce K. Gordon ◽  
Marty R. Jacobson
Keyword(s):  
Azotobacter Vinelandii ◽  
Nitrogenase Activity ◽  
Resistant Mutant ◽  
Free Medium ◽  
Wild Type ◽  
Isolation And Characterization ◽  
Mutant Strains ◽  
Resistant Strains ◽  
Resistant Mutants

Mutant strains of Azotobacter vinelandii which might have potential for use as bacterial fertilizer have been isolated and fall into two categories: constitutive mutants that synthesize nitrogenase in the presence of ammonium and mutants that overproduce nitrogenase when grown in nitrogen-free medium. The constitutive mutants described in this paper were isolated from the wild type as methylalanine-resistant strains and express up to 23% of the fully derepressed nitrogenase level when grown in medium containing excess ammonium. By contrast, ammonium-grown cultures of wild type have less than 0.003% of the fully derepressed level. Strains which fix more N2 than the wild type in nitrogen-free medium were isolated as mefhylammonium-resistant mutants. Although the methylammonium-resistant mutant strains fix more N2 than the wild type, they grow no faster. The excess nitrogen produced by these mutants is excreted into the medium, resulting in up to 60% more nitrogen than in the medium of the wild type. Higher nitrogenase activity in the methylammonium-resistant mutant strains was found to be a result of increased levels of nitrogenase protein, suggesting that regulation of nitrogenase synthesis may be altered.

Glutamate synthase levels in Neurospora crassa mutants altered with respect to nitrogen metabolism

1981 ◽  
Vol 1 (2) ◽  
pp. 158-164
Author(s):  
N S Dunn-Coleman ◽  
E A Robey ◽  
A B Tomsett ◽  
R H Garrett
Keyword(s):  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Glutamate Synthase ◽  
Wild Type ◽  
Mutant Strains ◽  
Synthase Regulation ◽  
Glutamate Biosynthesis ◽  
Glutamine Limitation

Glutamate synthase catalyzes glutamate formation from 2-oxoglutarate plus glutamine and plays an essential role when glutamate biosynthesis by glutamate dehydrogenase is not possible. Glutamate synthase activity has been determined in a number of Neurospora crassa mutant strains with various defects in nitrogen metabolism. Of particular interest were two mutants phenotypically mute except in an am (biosynthetic nicotinamide adenine dinucleotide phosphate-glutamate dehydrogenase deficient, glutamate requiring) background. These mutants, i and en-am, are so-called enhancers of am; they have been redesignated herein as en(am)-1 and en(am)-2, respectively. Although glutamate synthase levels in en(am)-1 were essentially wild type, the en(am)-2 strain was devoid of glutamate synthase activity under all conditions examined, suggesting that en(am)-2 may be the structural locus for glutamate synthase. Regulation of glutamate synthase occurred to some extent, presumably in response to glutamate requirements. Glutamate starvation, as in am mutants, led to enhanced activity. In contrast, glutamine limitation, as in gln-1 mutants, depressed glutamate synthase levels.

scholarly journals Limited Role of Secreted Aspartyl Proteinases Sap1 to Sap6 in Candida albicans Virulence and Host Immune Response in Murine Hematogenously Disseminated Candidiasis

2010 ◽  
Vol 78 (11) ◽  
pp. 4839-4849 ◽  
Author(s):  
Alexandra Correia ◽  
Ulrich Lermann ◽  
Luzia Teixeira ◽  
Filipe Cerca ◽  
Sofia Botelho ◽  
...  
Keyword(s):  
Immune Response ◽  
Candida Albicans ◽  
Significant Role ◽  
Murine Model ◽  
Null Mutant ◽  
Wild Type ◽  
Survival Times ◽  
Disseminated Candidiasis ◽  
Mutant Strains ◽  
Aspartyl Proteinases

ABSTRACTCandida albicanssecreted aspartyl proteinases (Saps) are considered virulence-associated factors. Several members of the Sap family were claimed to play a significant role in the progression of candidiasis established by the hematogenous route. This assumption was based on the observed attenuated virulence ofsap-null mutant strains. However, the exclusive contribution ofSAPgenes to their attenuated phenotype was not unequivocally confirmed, as the Ura status of these mutant strains could also have contributed to the attenuation. In this study, we have reassessed the importance ofSAP1toSAP6in a murine model of hematogenously disseminated candidiasis usingsap-null mutant strains not affected in theirURA3gene expression and compared their virulence phenotypes with those of Ura-blastersapmutants. The median survival time of BALB/c mice intravenously infected with a mutant strain lackingSAP1toSAP3was equivalent to that of mice infected with wild-type strain SC5314, while those infected with mutant strains lackingSAP5showed slightly extended survival times. Nevertheless, no differences could be observed between the wild type and a Δsap456mutant in their abilities to invade mouse kidneys. Likewise, a deficiency inSAP4toSAP6had no noticeable impact on the immune response elicited in the spleens and kidneys ofC. albicans-infected mice. These results contrast with the behavior of equivalent Ura-blaster mutants, which presented a significant reduction in virulence. Our results suggest that Sap1 to Sap6 do not play a significant role inC. albicansvirulence in a murine model of hematogenously disseminated candidiasis and that, in this model, Sap1 to Sap3 are not necessary for successfulC. albicansinfection.

scholarly journals Glutamate synthase levels in Neurospora crassa mutants altered with respect to nitrogen metabolism.

1981 ◽  
Vol 1 (2) ◽  
pp. 158-164 ◽  
Author(s):  
N S Dunn-Coleman ◽  
E A Robey ◽  
A B Tomsett ◽  
R H Garrett
Keyword(s):  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Nitrogen Metabolism ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Glutamate Synthase ◽  
Wild Type ◽  
Mutant Strains ◽  
Synthase Regulation ◽  
Glutamate Biosynthesis ◽  
Glutamine Limitation

Glutamate synthase catalyzes glutamate formation from 2-oxoglutarate plus glutamine and plays an essential role when glutamate biosynthesis by glutamate dehydrogenase is not possible. Glutamate synthase activity has been determined in a number of Neurospora crassa mutant strains with various defects in nitrogen metabolism. Of particular interest were two mutants phenotypically mute except in an am (biosynthetic nicotinamide adenine dinucleotide phosphate-glutamate dehydrogenase deficient, glutamate requiring) background. These mutants, i and en-am, are so-called enhancers of am; they have been redesignated herein as en(am)-1 and en(am)-2, respectively. Although glutamate synthase levels in en(am)-1 were essentially wild type, the en(am)-2 strain was devoid of glutamate synthase activity under all conditions examined, suggesting that en(am)-2 may be the structural locus for glutamate synthase. Regulation of glutamate synthase occurred to some extent, presumably in response to glutamate requirements. Glutamate starvation, as in am mutants, led to enhanced activity. In contrast, glutamine limitation, as in gln-1 mutants, depressed glutamate synthase levels.

ALS3 and ALS8 represent a single locus that encodes a Candida albicans adhesin; functional comparisons between Als3p and Als1p

Microbiology ◽  
2004 ◽  
Vol 150 (7) ◽  
pp. 2415-2428 ◽  
Author(s):  
Xiaomin Zhao ◽  
Soon-Hwan Oh ◽  
Georgina Cheng ◽  
Clayton B. Green ◽  
Jennifer A. Nuessen ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Germ Tube ◽  
Fluorescent Protein ◽  
Mutational Analysis ◽  
Oral Candidiasis ◽  
Tube Formation ◽  
Single Locus ◽  
Wild Type ◽  
Mutant Strains ◽  
Encoded Proteins

The ALS (agglutinin-like sequence) gene family of Candida albicans encodes eight cell-surface glycoproteins, some of which are involved in adherence to host surfaces. A mutational analysis of each ALS gene is currently being performed to deduce the functions of the encoded proteins and to better understand the role of these proteins in C. albicans biology and pathogenesis. This paper describes construction of an als3/als3 mutant and comparison of its phenotype to an als1/als1 strain. Efforts to disrupt ALS3 indicated that the gene could be deleted in two transformation steps, suggesting that the gene is encoded by a single locus and that the ALS3-like locus, ALS8, does not exist. Strains lacking ALS3 or ALS1 did not exhibit a defect in germ tube formation when grown in RPMI 1640 medium, but the als1/als1 mutant formed significantly fewer germ tubes in Lee medium. Analysis of ALS3 and ALS1 promoter activity using green fluorescent protein (GFP) reporter strains and flow cytometry showed that when cells are placed into medium that promotes germ tube formation, ALS1 is transcribed prior to ALS3. Comparison of the mutant strains in adhesion assays showed that the als3/als3 strain was defective in adhesion to both human umbilical vein endothelial cells (HUVEC) and buccal epithelial cells (BEC), but not to fibronectin-coated plastic plates. In contrast, the als1/als1 strain showed decreased adherence to HUVEC, but adherence to BEC and fibronectin were the same as wild-type controls. Inoculation of the buccal reconstituted human epithelium (RHE) model of oral candidiasis with the mutant strains showed nearly a total lack of adhesion and epithelial destruction by the als3/als3 mutant while the als1/als1 strain showed only a slightly reduced degree of epithelial destruction compared to the wild-type control. Adhesion data presented here suggest that, in the assays performed, loss of Als3p affects C. albicans adhesion more than loss of Als1p. Collectively, these results demonstrate functional similarities and differences between Als1p and Als3p, and suggest the potential for more complex interrelationships between the ALS genes and their encoded proteins.

scholarly journals Deletion of the Dynein Heavy-Chain Gene DYN1 Leads to Aberrant Nuclear Positioning and Defective Hyphal Development in Candida albicans

2004 ◽  
Vol 3 (6) ◽  
pp. 1574-1588 ◽  
Author(s):  
R. Martin ◽  
A. Walther ◽  
J. Wendland
Keyword(s):  
Candida Albicans ◽  
Heavy Chain ◽  
Time Lapse ◽  
Yeast Cells ◽  
Chain Gene ◽  
Wild Type ◽  
Heavy Chain Gene ◽  
Mutant Strains ◽  
Mutant Phenotypes

ABSTRACT Cytoplasmic dynein is a microtubule-associated minus-end-directed motor protein. CaDYN1 encodes the single dynein heavy-chain gene of Candida albicans. The open reading frames of both alleles of CaDYN1 were completely deleted via a PCR-based approach. Cadyn1 mutants are viable but grow more slowly than the wild type. In vivo time-lapse microscopy was used to compare growth of wild-type (SC5314) and dyn1 mutant strains during yeast growth and after hyphal induction. During yeast-like growth, Cadyn1 strains formed chains of cells. Chromosomal TUB1-GFP and HHF1-GFP alleles were used both in wild-type and mutant strains to monitor the orientation of mitotic spindles and nuclear positioning in C. albicans. In vivo fluorescence time-lapse analyses with HHF1-GFP over several generations indicated defects in dyn1 cells in the realignment of spindles with the mother-daughter axis of yeast cells compared to that of the wild type. Mitosis in the dyn1 mutant, in contrast to that of wild-type yeast cells, was very frequently completed in the mother cells. Nevertheless, daughter nuclei were faithfully transported into the daughter cells, resulting in only a small number of multinucleate cells. Cadyn1 mutant strains responded to hypha-inducing media containing l-proline or serum with initial germ tube formation. Elongation of the hyphal tubes eventually came to a halt, and these tubes showed a defect in the tipward localization of nuclei. Using a heterozygous DYN1/dyn1 strain in which the remaining copy was controlled by the regulatable MAL2 promoter, we could switch between wild-type and mutant phenotypes depending on the carbon source, indicating that the observed mutant phenotypes were solely due to deletion of DYN1.

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