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Titolo:
Proton translocating ATPase mediated fungicidal activity of a novel complex carbohydrate: CAN-296
Autore:
Ben-Josef, AM; Manavathu, EK; Platt, D; Sobel, JD;
Indirizzi:
Wayne State Univ, Dept Med, Div Infect Dis, Detroit, MI 48201 USA Wayne State Univ Detroit MI USA 48201 v Infect Dis, Detroit, MI 48201 USA Safe Sci, Boston, MA USA Safe Sci Boston MA USASafe Sci, Boston, MA USA
Titolo Testata:
INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS
fascicolo: 4, volume: 13, anno: 2000,
pagine: 287 - 295
SICI:
0924-8579(2000)13:4<287:PTAMFA>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
BONE-MARROW TRANSPLANTATION; PLASMA-MEMBRANE ATPASE; INVASIVE ASPERGILLOSIS; H+-ATPASE; FUNGAL-INFECTIONS; CANDIDA-ALBICANS; RESISTANCE; AIDS; EPIDEMIOLOGY; EVOLUTION;
Keywords:
antifungal agent; fungal infection; complex carbohydrate; H+-ATPase; Candida;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Manavathu, EK Wayne State Univ, Dept Med, Div Infect Dis, 427 Lande Bldg,550 E Canfield,Detroit, MI 48201 USA Wayne State Univ 427 Lande Bldg,550 E Canfield Detroit MI USA 48201
Citazione:
A.M. Ben-Josef et al., "Proton translocating ATPase mediated fungicidal activity of a novel complex carbohydrate: CAN-296", INT J ANT A, 13(4), 2000, pp. 287-295

Abstract

CAN-296 is a complex carbohydrate (approximately 4300 Da) isolated from the cell wall of Mucor rouxii. It exhibits excellent in vitro fungicidal activity against a wide spectrum of pathogenic yeasts, including isolates resistant to azoles and polyenes. The rapid irreversible action of CAN-296 on intact fungal cells and protoplasts suggested a membrane-located target for its action. The proton translocating ATPase (H+-ATPase) of fungi is an essential enzyme required for the regulation of intracellular pH and nutrient transport. Inhibition of H+-ATPase leads to intracellular acidification and cell death. We therefore investigated the effect of CAN-296 on H+-ATPase-mediated proton pumping by intact cells of Candida and Saccharomyces species by measuring the glucose-induced acidification of external medium. CAN-296 inhibited proton pumping of Candida albicans, Candida glabrata, Candida krusei, Candida guilliermondii and Saccharomyces cerevisiae at low concentrations (0.075-1.25 mg/l). Other commonly used antifungal agents such as amphotericin B, itraconazole and fluconazole had no effect on H+-ATPase-mediated proton primping. A clinical isolate of C. glabrata with reduced in vitro susceptibility (MIC = 10 mg/l) to CAN-296 also showed resistance to CAN-296 inhibition of proton pumping. Purified membrane fractions rich in H+-ATPase activity were not inhibited by CAN-296 suggesting that the effect on the H+-ATPase-mediated proton pumping in intact yeast cells is an indirect effect,perhaps mediated by local or global disruption of the plasma membrane. These results suggest that the inhibition of fungal Ht-ATPase is at least partly responsible for the antifungal activity of CAN-296. (C) 2000 Elsevier Science B.V. and International Society of Chemotherapy. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 19:59:14