Lipids in the Structure and Function of Fungal Membranes

Lösel, Dorothy M.

doi:10.1007/978-3-642-74215-6_9

Cited by 31 publications

(21 citation statements)

References 42 publications

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“…These findings are in agreement with the results of chitin synthase from S. cerevisiae [5], C. albicans [17], and other membrane-bound enzymes such as ATPase [2]. Although sterols have been suggested to contribute to the stability of fungal membranes [11] and to play a role in chitin synthase activity [18], activity was unaffected by sterols in vitro (Table 3). Ergosterol, a characteristic sterol in zygomycetes [11], had no effect on chitin synthase activity in the present study as well as in other studies [5,6].…”

Section: Resultssupporting

confidence: 90%

“…1). No other phospholipids such as PE, or PS had this effect, so PI, a common phospholipid in fungal membranes [11], plays a specific role in activating chitin synthase as found in S. commune [6]. It was demonstrated that the changes of the inositolcontaining lipids in the inl mutant of N. crassa led to an aberrant hyphal morphology and changes in the composition of the cell wall [3].…”

Section: Resultsmentioning

confidence: 99%

“…However, there are no reports of activation of membrane-bound enzyme by phospholipids which have a 20:4 fatty acyl moiety attached to the sn-2 glycerol carbon. In the lower fungi, including zygomycetes, the broadest spectrum of fatty acid composition occurs with substantial amounts of polyunsaturated C20 fatty acids [11]. A 20:4 chain attached to the polar region of phospholipids is said to enhance membrane fluidity [16], suggesting that this chain may act on chitin synthase.…”

Section: Resultsmentioning

confidence: 99%

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Phospholipid requirements of membrane-bound chitin synthase from Absidia glauca

Machida

1994

FEMS Microbiology Letters

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Membrane-bound chitin synthase, a key enzyme in chitin biosynthesis, had a specific requirement for phospholipid. The activity of the enzyme was enhanced 2.7-fold by adding phosphatidylinositol from porcine liver but not by other phospholipids. Each of the constituents of phospholipids inhibited enzyme activity at concentrations over 0.05%. Sterols and glycolipids had little effect on chitin synthase activation. Moreover, investigation using defined species of phosphatidylcholine revealed that 1-palmytoyl-2-arachidoyl and 1-stearoyl-2-arachidoyl phosphatidylcholine activated the enzyme. In contrast to the arachidoyl acyl chain, other species having unsaturated fatty acyl chains inhibited enzyme activity at a concentration of 0.01%.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Phospholipid requirements of membrane-bound chitin synthase from Absidia glauca

Machida

1994

FEMS Microbiology Letters

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“…Experimentally, it was observed that cultures in acid medium showed a reduced mycelial growth. This variation is attributable to increased synthesis of saturated fatty acids (i.e., 16C:0 and 18C:0) that increase the rigidity of the cell membrane and make it less fluid, in order to maintain proper cell function during conditions of stress (Lösel 1990). …”

Section: Discussionmentioning

confidence: 99%

Variation of sterols and fatty acids as an adaptive response to changes in temperature, salinity and pH of a marine fungus Epicoccum nigrum isolated from the Patagonian Fjords

Ahumada-Rudolph¹,

Cajas-Madriaga²,

Rudolph

et al. 2014

Rev. biol. mar. oceanogr.

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“…However, resistance to echinocandin-like antibiotics in C. albicans has been attributed to changes in membrane composition (22). Since PC is the major phospholipid of S. cerevisiae and C. albicans (20), we used PC SUVs as a model system to show the interaction of cilofungin with membrane components. Minor changes in membrane composition between S. cerevisiae and C. albicans could potentiate the mode of action of echinocandin-like antibiotics.…”

Section: Materuils and Methodsmentioning

confidence: 99%

Use of cilofungin as direct fluorescent probe for monitoring antifungal drug-membrane interaction

Ludescher

Frost

et al. 1994

Antimicrob Agents Chemother

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Cilofungin is an antifungal cyclopeptide which inhibits cell wall (1,3)-p1-glucan biosynthesis in fungal organisms, and its action against Candida albicans (1,3)-Il-glucan synthase has been widely studied. Since glucan synthase inactivation is thought to partially result from perturbations of the membrane lipid environment, the interaction of cilofungin with fungal membranes and phosphatidylcholine membrane vesicles was studied. Cilofungin, which contains two independent aromatic groups, has an excitation maximum of 270 nm and an emission maximum of 317 nm in aqueous solution. Comparison of the fluorescence properties of cilofungin with those of the analogs pneumocandin Bo, N-acetyl-tyrosinamide, and 4-hydroxybenzamide indicated that the emission of cilofungin largely derived from the p-octyloxybenzamide side chain. Microsomal membranes from Saccharomyces cerevisiae, C. albicans, and phosphatidylcholine membrane vesicles induced a blue shift in the cilofungin emission spectrum and increased the cilofungin steady-state emission anisotropy, providing direct evidence for a cilofungin-membrane interaction. Cilofungin interacted more strongly with membranes of C. albicans than with those of S. cerevisiae, correlating with previous findings that C. albicans is far more susceptible than S. cerevisiae to the action of cilofungin. These findings support the hypothesis that drug-induced inhibition of the (1,3)-,B-glucan synthesis results from the perturbation of the membrane environment and the interaction with the glucan synthase complex combined. The study demonstrated ways in which the fluorescence properties of drugs can be used to directly evaluate drug-membrane interactions and structure-activity relationships.New antifungal drugs that are directed against specific fungal targets and that cause minimal toxicity to the host have attracted considerable interest in recent years. One such target is the plasma membrane-localized (1,3)-3-glucan synthase (GS; EC 2.4.1.34), which catalyzes the biosynthesis of (1,3)-1-glucan, an essential structural polymer of the cell wall (17,36). A number of antifungal drugs have been targeted against GSs from various fungi including the lipopeptide echinocandin-like class of inhibitors (12,30,31,35), aculeacin A (23, 24), cilofungin (8, 10, 11), pneumocandins (12, 31), and the papulacandins (2, 16, 26, 37), which are lipid-like saccharides. Each of these compounds contains fatty acid side chains, which have been shown to be essential for the actions of cilofungin (34,38) and papulacandin B (37). Although various lipophilic compounds are known to rapidly inactivate fungal glucan (18,25) and chitin synthases (25), the mechanism by which these compounds interfere with GS has only recently begun to attract considerable attention (17,18,36).Drug-membrane interactions can be probed directly by fluorescence spectroscopic techniques, provided that the drug contains a structural moiety exhibiting fluorescence properties (6, 7). In the present study, we demonstrated that cilofungin, which contains...

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Lipids in the Structure and Function of Fungal Membranes

Cited by 31 publications

References 42 publications

Phospholipid requirements of membrane-bound chitin synthase from Absidia glauca

Phospholipid requirements of membrane-bound chitin synthase from Absidia glauca

Variation of sterols and fatty acids as an adaptive response to changes in temperature, salinity and pH of a marine fungus Epicoccum nigrum isolated from the Patagonian Fjords

Use of cilofungin as direct fluorescent probe for monitoring antifungal drug-membrane interaction

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