Nystatin changes the properties of transporters for arginine and sugars An in vitro study

Opekarová, Miroslava; Tanner, Widmar

doi:10.1016/0014-5793(94)00730-6

Cited by 20 publications

(12 citation statements)

References 16 publications

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“…This is supported by the observation that nystatin affected properties of the arginine and glucose transporters in yeast plasma membrane vesicles (20). Further, the amphotericin B methyl ester inhibited the replication, assembly, and release of HIV-1 by interfering with the ion channel viral protein U (VPU) (18,21).…”

Section: Discussionmentioning

confidence: 83%

Polyene antibiotic that inhibits membrane transport proteins

Welscher

Leeuwen

Kruijff

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The limited therapeutic arsenal and the increase in reports of fungal resistance to multiple antifungal agents have made fungal infections a major therapeutic challenge. The polyene antibiotics are the only group of antifungal antibiotics that directly target the plasma membrane via a specific interaction with the main fungal sterol, ergosterol, often resulting in membrane permeabilization. In contrast to other polyene antibiotics that form pores in the membrane, the mode of action of natamycin has remained obscure but is not related to membrane permeabilization. Here, we demonstrate that natamycin inhibits growth of yeasts and fungi via the immediate inhibition of amino acid and glucose transport across the plasma membrane. This is attributable to ergosterol-specific and reversible inhibition of membrane transport proteins. It is proposed that ergosterol-dependent inhibition of membrane proteins is a general mode of action of all the polyene antibiotics, of which some have been shown additionally to permeabilize the plasma membrane. Our results imply that sterol-protein interactions are fundamentally important for protein function even for those proteins that are not known to reside in sterol-rich domains.

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Section: Discussionmentioning

confidence: 83%

Polyene antibiotic that inhibits membrane transport proteins

Welscher

Leeuwen

Kruijff

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…A sample taken at the time of infection served as a baseline. Samples were collected at 10,20,30,45,60, and 90 min p.i., and infection was stopped by adding an equal volume of 10% TCA. Samples were processed for radiometric analysis as described above.…”

Section: Methodsmentioning

confidence: 99%

Chlorovirus-Mediated Membrane Depolarization ofChlorellaAlters Secondary Active Transport of Solutes

Agarkova

Dunigan

Gurnon

et al. 2008

J Virol

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Paramecium bursaria chlorella virus 1 (PBCV-1) is the prototype of a family of large, double-stranded DNA, plaque-forming viruses that infect certain eukaryotic chlorella-like green algae from the genus Chlorovirus. PBCV-1 infection results in rapid host membrane depolarization and potassium ion release. One interesting feature of certain chloroviruses is that they code for functional potassium ion-selective channel proteins (Kcv) that are considered responsible for the host membrane depolarization and, as a consequence, the efflux of potassium ions. This report examines the relationship between cellular depolarization and solute uptake. Annotation of the virus host Chlorella strain NC64A genome revealed 482 putative transporter-encoding genes; 224 are secondary active transporters. Solute uptake experiments using seven radioactive compounds revealed that virus infection alters the transport of all the solutes. However, the degree of inhibition varied depending on the solute. Experiments with nystatin, a drug known to depolarize cell membranes, produced changes in solute uptake that are similar but not identical to those that occurred during virus infection. Therefore, these studies indicate that chlorovirus infection causes a rapid and sustained depolarization of the host plasma membrane and that this depolarization leads to the inhibition of secondary active transporters that changes solute uptake.

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“…In any case, its result is obviously a change in the functional state of the transport proteins, as seen in physiological studies which demonstrated that nystatin caused changes in the properties of transport systems reconstituted in ergosterol-containing vesicles. Nystatin binding to ergosterol in the vicinity of an amino acid permease released this yeast transporter from its coupling to energy and converted it to a facilitator [11]. A more defined system (e.g.…”

Section: Resultsmentioning

confidence: 99%

“…Arginine accumulation in the vesicles is driven by protonmotive force (pmf); however, even when the pmf is completely abolished by low concentrations of uncouplers no efflux of accumulated arginine occurs [11]. This finding reflects the unidirectionality of amino acid transport observed in whole yeast cells (for review see, e.g.…”

Section: Introductionmentioning

confidence: 99%

“…Recently we examined the effect of nystatin on the transport of arginine in an in vitro system of yeast plasma membrane vesicles which eliminates the interference of cellular compartmentation [11] and offers the possibility to change nearly arbitrarily the membrane lipid composition. Arginine accumulation in the vesicles is driven by protonmotive force (pmf); however, even when the pmf is completely abolished by low concentrations of uncouplers no efflux of accumulated arginine occurs [11].…”

Section: Introductionmentioning

confidence: 99%

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