Cited by 612Antifungal resistance and susceptibilityAntimicrobial agents and applicationsLipid Membrane Structure and Behavior

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Amphotericin primarily kills yeast by simply binding ergosterol

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Gray, Kaitlyn C., Palacios, Daniel S., Dailey, Ian, Endo, Matthew M., Uno, Brice E., Wilcock, Brandon C., Burke, Martin D.·2012·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1117280109PMC PMC3289339

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Abstract

Amphotericin B (AmB) is a prototypical small molecule natural product that can form ion channels in living eukaryotic cells and has remained refractory to microbial resistance despite extensive clinical utilization in the treatment of life-threatening fungal infections for more than half a century. It is now widely accepted that AmB kills yeast primarily via channel-mediated membrane permeabilization. Enabled by the iterative cross-coupling-based synthesis of a functional group deficient derivative of this natural product, we have discovered that channel formation is not required for potent fungicidal activity. Alternatively, AmB primarily kills yeast by simply binding ergosterol, a lipid that is vital for many aspects of yeast cell physiology. Membrane permeabilization via channel formation represents a second complementary mechanism that further increases drug potency and the rate of yeast killing. Collectively, these findings ( i ) reveal that the binding of a physiologically important microbial lipid is a powerful and clinically validated antimicrobial strategy that may be inherently refractory to resistance, ( ii ) illuminate a more straightforward path to an improved therapeutic index for this clinically vital but also highly toxic antifungal agent, and ( iii ) suggest that the capacity for AmB to form protein-like ion channels might be separable from its cytocidal effects.

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Authors: Gray, K. C., Palacios, D. S., Dailey, I., Endo, M. M., Uno, B. E., Wilcock, B. C., & Burke, M. D.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Gray, Kaitlyn C.
Palacios, Daniel S.
Burke, Martin D.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2012-01-17
Volume: 109
Issue: 7
Pages: 2234-2239
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1117280109
PMC: PMC3289339
OpenAlex: W1987640473
Cited by: 608
References: 50
Citations by year: 2026: 42 · 2025: 42 · 2024: 34 · 2023: 49 · 2022: 45 · 2021: 56 · 2020: 53 · 2019: 50 · 2018: 32 · 2017: 44 · 2016: 44 · 2015: 40 · 2014: 36 · 2013: 30 · 2012: 11
FWCI: 24.34
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
Bristol-Myers Squibb
National Institutes of Health
National Institute of General Medical Sciences (R01GM080436, GM080436)
Topics: Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords: amphotericin B, ergosterol binding, yeast cell death, antifungal mechanism, ion channel formation, membrane permeabilization, fungal drug resistance, natural product derivatives, therapeutic index, antifungal toxicity
MeSH terms: Amphotericin B, Antifungal Agents, Ergosterol, Saccharomyces cerevisiae

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Amphotericin primarily kills yeast by simply binding ergosterol

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