Venturicidin: A New Antifungal Antibiotic of Potential Use in Agriculture

Rhodes, A.; Fantes, K. H.; Boothroyd, B.; McGONAGLEMP,; Crosse, Rosemary

doi:10.1038/192952a0

Cited by 56 publications

(34 citation statements)

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“…1959), seems to be the best antifungal substance among the 300 or more analogues tested for potential use ah plant protectants ; in our tests it showed improved activity in vitro and in vivo, exhibited local systemic action as a foliage spray, gave a good performance against apple scab ( Venturia inaequalis) and provided excellent control of chrysanthemum mildew (Oidium chrysanthemi) in greenhouse tests. The activity of the 2'-propoxy analogue of griseofulvin (R 10/122) against apple scab was, however, much inferior to that of the antibiotic venturicidin (Rhodes et al 1961), and it should be noted that complete control of chrysanthemum mildew has already been obtained by root-watering with griseofulvin itself (Rhodes, 1962). Having regard to the increased cost relative to griseofulvin, the outlook for practical use of analogue R 101122 must be considered to be unfavourable.…”

Section: Discussionmentioning

confidence: 99%

Some Relations between Chemical Structure and Antifungal Effects of Griseofulvin Analogues

Crosse¹,

McWilliam²,

Rhodes³

1964

Journal of General Microbiology

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SUMMARYInhibitory effects of more than 300 analogues of griseofulvin against six dermatophytic fungi and eight plant pathogenic fungi were determined in an investigation of relations between chemical structure and biological activity. The influence of chemical structure on physical properties of the analogues appeared dominant, but optimum requirements for in vitro performance were somewhat different from those required in vivo for effective control of plant pathogenic or dermatophytic fungi.

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Section: Discussionmentioning

confidence: 99%

Some Relations between Chemical Structure and Antifungal Effects of Griseofulvin Analogues

Crosse¹,

McWilliam²,

Rhodes³

1964

Journal of General Microbiology

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“…Some natural macrolides, apoptolidin, cytovaricin, oligomycin, ossamycin, and venturicidin are elaborated by Nocardiopsis spp. and various strains of Streptomyces and are known as potent inhibitors of ATP synthase (Table 8) (205,207,225,330,358,359). The binding sites of the macrolide inhibitors are located within the F 0 part of the complex.…”

Section: Polyketide Inhibitorsmentioning

confidence: 99%

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Hong

Pedersen

2008

Microbiol Mol Biol Rev

275

302

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SUMMARY ATP synthase, a double-motor enzyme, plays various roles in the cell, participating not only in ATP synthesis but in ATP hydrolysis-dependent processes and in the regulation of a proton gradient across some membrane-dependent systems. Recent studies of ATP synthase as a potential molecular target for the treatment of some human diseases have displayed promising results, and this enzyme is now emerging as an attractive molecular target for the development of new therapies for a variety of diseases. Significantly, ATP synthase, because of its complex structure, is inhibited by a number of different inhibitors and provides diverse possibilities in the development of new ATP synthase-directed agents. In this review, we classify over 250 natural and synthetic inhibitors of ATP synthase reported to date and present their inhibitory sites and their known or proposed modes of action. The rich source of ATP synthase inhibitors and their known or purported sites of action presented in this review should provide valuable insights into their applications as potential scaffolds for new therapeutics for human and animal diseases as well as for the discovery of new pesticides and herbicides to help protect the world's food supply. Finally, as ATP synthase is now known to consist of two unique nanomotors involved in making ATP from ADP and Pi, the information provided in this review may greatly assist those investigators entering the emerging field of nanotechnology.

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“…Methods for mitochondrial isolation, sub-mitochondrial particles, F,-ATPase, oligomycin-sensitivity-conferring protein and oligomycin-sensitive ATPase isolation as well as assay methods for ATPase and protein and gel electrophoresis techniques are as described previously [6,12,14]. Sensitivity of mitochondrial ATPase to inhibitors are listed as I,, values (pg inhibitor/mg protein), defined as the amount of inhibitor required to reduce activity to 50% of maximal.…”

Section: Enzyme Isolation and Assay Methodsmentioning

confidence: 99%

“…One important criterion in the isolation of specific mutants resistant to inhibitors and uncouplers of the Growth of parental strain D22 was assayed turbidimetrically as described previously [I21 on ethanol medium (A) or mitochondrial energy conservation system has been to establish that the drug has a specific effect on mitochondrial energy conservation processes [6,7,15]. Venturicidin satisfies this criterion in that growth on solid media is inhibited at 0.1 pg/ml when glycerol or ethanol is the carbon source but growth is unaffected at 30pg/ml when glucose is the carbon source and glycolytic fermentation is the main energy supply for cell growth.…”

Section: Specijicity Of Venturicidin For Aerobic Growthmentioning

confidence: 99%

Studies on Energy-Linked Reactions: Isolation and Properties of Mitochondrial Venturicidin-Resistant Mutants of Saccharomyces cerevisiae

et al. 1975

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Venturicidin is a specific inhibitor of aerobic growth of yeast and has no effect on fermentative growth, a result which is consistent with its known mode of action on mitochondrial oxidative phosphorylation. Venturicidin‐resistant mutants of Saccharomyces cerevisiae have been isolated and form two general classes: class 1, nuclear mutants which are resistant to a variety of mitochondrial inhibitors and uncouplers, and class 2, mitochondrial mutants of phenotype VENR OLYR and VENR TETRin vivo. VENR OLYR mutants show a high degree of resistance to venturicidin and oligomycin at the whole cell and mitochondrial ATPase level but, in contrast, no resistance at the mitochondrial level is observed with VENR TETR mutants. Venturicidin resistance/sensitivity can be correlated with two binding sites on mitochondrial ATPase, one of which is common to the oligomycin binding site and the other is common to the triethyl tin binding site. Biochemical genetic studies indicate that two mitochondrial genes specify venturicidin resistance/sensitivity and that the mitochondrial gene products are components of the mitochondrial ATPase complex.

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Venturicidin: A New Antifungal Antibiotic of Potential Use in Agriculture

Cited by 56 publications

References 1 publication

Some Relations between Chemical Structure and Antifungal Effects of Griseofulvin Analogues

Some Relations between Chemical Structure and Antifungal Effects of Griseofulvin Analogues

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Studies on Energy-Linked Reactions: Isolation and Properties of Mitochondrial Venturicidin-Resistant Mutants of Saccharomyces cerevisiae

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