Echinocandin resistance in Candida.

Perlin, David S.

doi:10.1093/cid/civ791

Cited by 374Antifungal resistance and susceptibilityFungal and yeast genetics researchFungal Plant Pathogen Control

Echinocandin resistance in Candida.

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Perlin, David S.·2015·Clinical Infectious Diseases

DOI 10.1093/cid/civ791PMC PMC4643482

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Abstract

Invasive fungal infections are an important infection concern for patients with underlying immunosuppression. Antifungal therapy is a critical component of patient care, but therapeutic choices are limited due to few drug classes. Antifungal resistance, especially among Candida species, aggravates the problem. The echinocandin drugs (micafungin, anidulafungin, and caspofungin) are the preferred choice to treat a range of candidiasis. They target the fungal-specific enzyme glucan synthase, which is responsible for the biosynthesis of a major cell wall polymer. Therapeutic failure involves acquisition of resistance, although it is a rare event among most Candida species. However, in some settings, higher-level resistance has been reported among Candida glabrata, which is also frequently resistant to azole drugs, resulting in difficult-to-treat multidrug-resistant strains. The mechanism of echinocandin resistance involves amino acid changes in "hot spot" regions of FKS-encoded subunits of glucan synthase, which decreases the sensitivity of enzyme to drug, resulting in higher minimum inhibitory concentration values. The cellular processes promoting the formation of resistant FKS strains involve complex stress response pathways that yield a variety of adaptive compensatory genetic responses. Standardized broth microdilution techniques can be used to distinguish FKS mutant strains from wild type, but testing C. glabrata with caspofungin should be approached cautiously. Finally, clinical factors that promote echinocandin resistance include prophylaxis, host reservoirs including biofilms in the gastrointestinal tract, and intra-abdominal infections. An understanding of clinical and molecular factors that promote echinocandin resistance is critical to develop better diagnostic tools and therapeutic strategies to overcome resistance.

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In echinocandin-tolerant Candida isolates, β-1,3- and β-1,6-glucan crosslink modifications and higher chitin content have been described.
“In echinocandin-tolerant Candida isolates, β-1,3- and β-1,6-glucans crosslinks modifications and higher chitin content have been described (Perlin, 2015), while higher β-D-glucan composition has been found in amphotericin-B-resistant Aspergillus flavus isolates (Seo et al., 1999).”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Perlin, 2015
The Drug Tolerance section describes increased chitin synthesis as a response to echinocandins and says Candida cell-wall mutants with elevated chitin are less susceptible. It does not describe modifications to β-1,3- and β-1,6-glucan crosslinks; it says only that chitin and glucans are biosynthetically interdependent. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Persistent echinocandin exposure leads to FKS mutations and organisms with marked and stable resistance emerge with a high chitin content in the cell wall.
“Eventually, persistent echinocandin exposure leads to FKS mutations and organisms with marked and stable resistance emerge with a high chitin content in the cell wall (Walker et al., 2013; Perlin, 2015).”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Perlin, 2015
The Risk Factors for Resistance Emergence section says resistance generally requires prolonged or repeated echinocandin exposure, though it can emerge rapidly. The Drug Tolerance section says tolerant cells can develop stable FKS mutations and higher-level resistance. It links elevated chitin to compensatory drug tolerance, however, not specifically to the organisms that emerge with stable FKS-mediated resistance. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The host environment and antifungal stress can lead to cell wall modifications related to drug resistance.
“The host environment and antifungal stress can lead to cell wall modifications related to drug resistance.”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Perlin, 2015
The Drug Tolerance section says echinocandin stress prompts compensatory chitin synthesis that strengthens the cell wall, and cells with elevated chitin are less susceptible to the drugs. The Risk Factors for Resistance Emergence section links host conditions, including gastrointestinal biofilms, to the emergence of resistant mutants, but does not say the host environment itself causes the cell-wall modifications. (LLM, conf=0.83)
Experimental — accuracy not yet measured
An intermediary step to antifungal resistance is the development of tolerance.
“An intermediary step to antifungal resistance is the development of tolerance (Perlin, 2015).”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Perlin, 2015
The Drug Tolerance section says echinocandin-tolerant Candida cells can develop higher-level resistance over time through stable FKS mutations. The Conclusions similarly say drug-adapted persister states may form resistant mutants. This supports tolerance as a possible intermediate state, but not as a necessary step for antifungal resistance generally. (LLM, conf=0.85)
Experimental — accuracy not yet measured
CSP treatment readily triggers cell wall integrity signaling involving several pathways and transcription factors, leading to cell wall remodeling and stress adaptations such as increased chitin exposure via the activation of chitin synthesis.
“In line with this, CSP treatment readily triggers cell wall integrity signaling involving several pathways and transcription factors, thus leading to cell wall remodeling and stress adaptations (55, 79) such as increased chitin exposure (80, 81) via the activation of chitin synthesis.”
From Transcriptomics and Phenotyping Define Genetic Signatures Associated with Echinocandin Resistance in Candida auris (2022) · cites this paper as [79]
Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measured

Resistance to echinocandins occurs naturally in C. auris strains and is increasing in C. albicans primarily due to mutations in two hotspot regions of β-1,3-glucan synthase Fks subunit.
“Resistance to echinocandins has been widely reported in C. auris strains, where it occurs naturally, and in C. albicans, where the incidence has been increasing primarily due to mutations in two hotspot regions of β−1,3-glucan synthase Fks subunit25,26.”
From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [25]
The FKS Mechanism of Resistance section (page not supplied) supports the two-hot-spot mechanism and describes resistance-conferring mutations in C. albicans. The Epidemiology section (page not supplied) says resistance remains below 3% in C. albicans and identifies C. glabrata—not C. albicans—as the species with rising resistance. Our copy does not establish that resistance occurs naturally in C. auris. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Extended echinocandin treatment is linked to the appearance of resistant strains.
“Of note, long periods of echinocandin therapy are associated with the emergence of echinocandin-resistant strains65.”
From Drug resistance and tolerance in fungi. (2020) · cites this paper as [65]
Echinocandin resistance results almost entirely from FKS gene mutations, which alter the drug target 1,3-β-glucan synthase.
“Echinocandin resistance is almost exclusively due to mutations in FKS genes (Table 1), which encode the target enzyme of the drug, 1,3-β-glucan synthase65.”
From Drug resistance and tolerance in fungi. (2020) · cites this paper as [65]
Cells surviving drug exposure can respond to selection and evolve resistance.
“Cells surviving drug exposure can respond to selection and evolve resistance (Perlin, 2015).”
From Fungal Cell Wall: Emerging Antifungals and Drug Resistance. (2019) · cites this paper as Perlin, 2015
A concern for echinocandin resistance in C. parapsilosis exists because of a naturally occurring variation in the protein target for echinocandins.
“Although a concern for echinocandin resistance in C. parapsilosis exists because of a naturally occurring variation in the protein target for echinocandins (61)”
From Population-Based Active Surveillance for Culture-Confirmed Candidemia — Four Sites, United States, 2012–2016 (2019) · cites this paper as [61]

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[7]7. Pfaller MA, Castanheira M, Lockhart SR, Ahlquist AM, Messer SA, Jones RN. Frequency of decreased susceptibility and resistance to echi- nocandins among fluconazole-resistant bloodstream isolates of Candi- da glabrata. J Clin Microbiol 2012; 50:1199-203.
[14]14. Johnson ME, Katiyar SK, Edlind TD. A new Fks hotspot for acquired echi- nocandin resistance in yeast, and its contribution to intrinsic resistance of Scedosporium species. Antimicrob Agents Chemother 2011; 55:3774-81.
[17]17. Arendrup MC, Perlin DS, Jensen RH, Howard SJ, Goodwin J, Hope W. Differential In vivo activity of anidulafungin, caspofungin and micafun- gin against C. glabrata with and without FKS resistance mutations. Antimicrob Agents Chemother 2012; 56:2435-42.
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Authors: Perlin, D. S.
Affiliations: Rutgers Health (US)
Corresponding author: Perlin, David S.
ORCID: Perlin, David S.
Venue: Clinical Infectious Diseases
Publisher: Oxford University Press (OUP)
Published: 2015-11-05
Volume: 61
Issue: suppl_6
Pages: S612-S617
ISSN: 1058-4838 (ISSN-L)
1537-6591
DOI: 10.1093/cid/civ791
PMC: PMC4643482
OpenAlex: W2231020609
Cited by: 374
References: 75
Citations by year: 2026: 45 · 2025: 48 · 2024: 28 · 2023: 26 · 2022: 31 · 2021: 47 · 2020: 43 · 2019: 43 · 2018: 23 · 2017: 29 · 2016: 9 · 2015: 1
FWCI: 16.09
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Clinical Infectious Diseases (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (AI069397, AI109025)
Topics: Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Fungal Plant Pathogen Control
Keywords: echinocandin resistance, Candida, Candida glabrata, glucan synthase, caspofungin, micafungin, anidulafungin, candidiasis, antifungal resistance, multidrug resistance, stress response pathways, biofilm, prophylaxis, intra-abdominal candidiasis, minimum inhibitory concentration
MeSH terms: Caspofungin, Micafungin, Anidulafungin, Antifungal Agents, Azoles, Candida, Candidiasis, Glucosyltransferases, Humans, Mutation, Drug Resistance, Multiple, Fungal, Candida glabrata, Echinocandins, Lipopeptides, Intraabdominal Infections

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