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Fungal phospholipase activity and susceptibility to lipid preparations of amphotericin B

M Gottfredsson1, C J Jessup, G M Cox

  • 1Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.

Antimicrobial Agents and Chemotherapy
|October 16, 2001
PubMed

Insights

Extracellular fungal phospholipase activity does not affect antifungal susceptibility testing for amphotericin B lipid complex (ABLC). This study utilized phospholipase-deficient fungal mutants to confirm findings in Candida albicans and Cryptococcus neoformans.

Area of Science:

  • Mycology
  • Antifungal Drug Discovery
  • Clinical Microbiology

Background:

  • Fungal phospholipases are enzymes that hydrolyze phospholipids.
  • Previous research suggested a potential role for fungal phospholipases in antifungal susceptibility testing.
  • Amphotericin B lipid complex (ABLC) is a crucial antifungal medication.

Purpose of the Study:

  • To investigate the influence of extracellular fungal phospholipase activity on the in vitro susceptibility of Candida albicans and Cryptococcus neoformans to amphotericin B lipid complex (ABLC).

Main Methods:

  • Utilized specific phospholipase-deficient mutants of Candida albicans and Cryptococcus neoformans.
  • Performed in vitro susceptibility testing comparing wild-type and mutant strains against ABLC.
  • Assessed the impact of extracellular phospholipase activity on ABLC efficacy.

Main Results:

  • Extracellular fungal phospholipase activity did not demonstrate a significant influence on the in vitro susceptibility of the tested fungal species to ABLC.
  • Results were consistent across both Candida albicans and Cryptococcus neoformans mutant strains.

Conclusions:

  • The study concludes that extracellular fungal phospholipase activity is not a confounding factor in the in vitro susceptibility testing of amphotericin B lipid complex (ABLC).
  • These findings support the reliability of current susceptibility testing methods for ABLC in the presence of common fungal phospholipases.

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