Candida albicans and Candida glabrata : global priority pathogens

Katsipoulaki, Myrto; Stappers, Mark H. T.; Malavia-Jones, Dhara; Brunke, Sascha; Hube, Bernhard; Gow, Neil A. R.

doi:10.1128/mmbr.00021-23

Cited by 180

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Candida albicans and Candida glabrata : global priority pathogens

Katsipoulaki, Myrto, Stappers, Mark H. T., Malavia-Jones, Dhara, Brunke, Sascha, Hube, Bernhard, Gow, Neil A. R.·2024·Microbiology and Molecular Biology Reviews

DOI 10.1128/mmbr.00021-23

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Abstract

SUMMARY: A significant increase in the incidence of Candida -mediated infections has been observed in the last decade, mainly due to rising numbers of susceptible individuals. Recently, the World Health Organization published its first fungal pathogen priority list, with Candida species listed in medium, high, and critical priority categories. This review is a synthesis of information and recent advances in our understanding of two of these species —Candida albicans and Candida glabrata . Of these, C. albicans is the most common cause of candidemia around the world and is categorized as a critical priority pathogen. C. glabrata is considered a high-priority pathogen and has become an increasingly important cause of candidemia in recent years. It is now the second most common causative agent of candidemia in many geographical regions. Despite their differences and phylogenetic divergence, they are successful as pathogens and commensals of humans. Both species can cause a broad variety of infections, ranging from superficial to potentially lethal systemic infections. While they share similarities in certain infection strategies, including tissue adhesion and invasion, they differ significantly in key aspects of their biology, interaction with immune cells, host damage strategies, and metabolic adaptations. Here we provide insights on key aspects of their biology, epidemiology, commensal and pathogenic lifestyles, interactions with the immune system, and antifungal resistance.

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GPI (glycosylphosphatidylinositol)-linked aspartyl proteases regulate vacuole homoeostasis in Candida glabrata
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The fungal pathogen Candida glabrata does not depend on surface ferric reductases for iron acquisition
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Pseudohyphae formation in Candida glabrata due to CO2 exposure
sassani, E., Division of Molecular Biology, D. O. M. M. A. P., Khodavaisy, S., Division of Molecular Biology, D. O. M. M. A. P., Agha Kuchak Afshari, S., Division of Molecular Biology, D. O. M. M. A. P., Darabian, S., Department of Medical Mycology and Parasitology, S. O. P. H., Aala, F., Department of Parasitology and Mycology, F. O. M., et al. (2016) · Current Medical Mycology · doi:10.18869/acadpub.cmm.2.4.49 · Cited by 27
Orchestrated actin nucleation by the Candida albicans polarisome complex enables filamentous growth
Xie, Y., Loh, Z. Y., Xue, J., Zhou, F., Sun, J., Qiao, Z., Jin, S., Deng, Y., Li, H., Wang, Y., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013890 · Cited by 26
Type I Interferons Ameliorate Zinc Intoxication of Candida glabrata by Macrophages and Promote Fungal Immune Evasion
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Candida albicans Interaction with Oral Epithelial Cells: Adhesion, Invasion, and Damage Assays
Mogavero, S., & Hube, B. (2021) · Methods in Molecular Biology · doi:10.1007/978-1-0716-1182-1_9 · Cited by 14
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200 of 443 shown

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Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR
Dickwella Widanage, M. C., Singh, K., Li, J., Yarava, J. R., Scott, F. J., Xu, Y., Gow, N. A. R., Mentink-Vigier, F., Wang, P., Lamoth, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61678-1 · Cited by 51
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Adaptive morphological changes link to poor clinical outcomes by conferring echinocandin tolerance in Candida tropicalis
Wu, Y., Zou, Y., Dai, Y., Lu, H., Zhang, W., Chang, W., Wang, Y., Nie, Z., Wang, Y., & Jiang, X. (2025) · PLOS Pathogens · doi:10.1371/journal.ppat.1013220 · Cited by 10
Echinocandin tolerance and persistence in vitro are regulated by calcineurin signaling in Candida glabrata
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Mitochondrial complex III subunit Qcr8 regulates the virulence and adhesion of Candida albicans by modulating mitochondrial function
Zhao, Q., Huang, X., Liu, Q., Cao, Y., Yu, X., Liu, Y., Hu, N., Han, Z., Tan, J., Li, X., et al. (2026) · Microbiology Spectrum · doi:10.1128/spectrum.01672-25

Authors: Katsipoulaki, M., Stappers, M. H. T., Malavia-Jones, D., Brunke, S., Hube, B., & Gow, N. A. R.
Venue: Microbiology and Molecular Biology Reviews
Publisher: American Society for Microbiology
Published: 2024-06-27
Volume: 88
Issue: 2
ISSN: 1092-2172
1098-5557
DOI: 10.1128/mmbr.00021-23
Cited by: 180
References: 91
Language: en
Licence: doi.org/10.1128/ASMCopyrightv2 (vor)
journals.asm.org/non-commercial-tdm-license (tdm)
Funders: Bundesministerium für Bildung und Forschung (13N15714, SAS-2015-HKI-LWC)
Deutsche Forschungsgemeinschaft (467 390713860, 528/20-1)
Wellcome Trust (101873, 200208, 215599, 224323)
UKRI | Medical Research Council (MR/M026663/2)
Medical Research Council Centre for Medical Mycology (MR/N006364/2)
National Institute for Health and Care Research Exeter Biomedical Research Centre
University of Exeter

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Candida albicans and Candida glabrata : global priority pathogens

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