Fungal ergosterol biosynthesis

Category: biosynthesis

Overview

Ergosterol is the fungal-specific membrane sterol (analog of mammalian cholesterol). Selective antifungal toxicity targets enzymes unique to fungi: azoles (fluconazole, itraconazole, voriconazole, posaconazole, ketoconazole, miconazole, clotrimazole) inhibit CYP51 (sterol-14α-demethylase) — depleting ergosterol + accumulating toxic 14α-methylsterols. Off-target hit on mammalian CYP3A4 explains the massive DDI surface for systemic azoles (itraconazole 20× midazolam AUC, etc.). Terbinafine + allylamines inhibit squalene epoxidase upstream → toxic squalene buildup. Hydroxypyridones (ciclopirox) chelate Fe/Al cofactors of multiple fungal enzymes. Polyenes (amphotericin B, nystatin) bind ergosterol directly → membrane pores.

Organ Systems

Pathway Steps

  1. lanosterol → ergosterol — via CYP51 (sterol-14α-demethylase) + downstream desaturases/reductases; azole-blockade target. Fungi convert lanosterol to ergosterol — their characteristic membrane sterol (the fungal analog of cholesterol) — via steps including CYP51 (14α-demethylase). Azole antifungals inhibit CYP51, and this fungal-specific sterol is what gives antifungals selectivity over human cells.
  2. squalene → lanosterol — via squalene epoxidase + lanosterol synthase; terbinafine blocks the epoxidase step. Earlier in the pathway, squalene is epoxidized (squalene epoxidase) and cyclized to lanosterol. Allylamines (terbinafine) inhibit squalene epoxidase, both depleting ergosterol and accumulating toxic squalene — a fungicidal action used for dermatophyte infections.

Known Modulators

References