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The Mnn2 Mannosyltransferase Family Modulates Mannoprotein Fibril Length, Immune Recognition and Virulence of Candida albicans
Open accessAbstract
The fungal cell wall is the first point of interaction between an invading fungal pathogen and the host immune system. The outer layer of the cell wall is comprised of GPI anchored proteins, which are post-translationally modified by both N- and O-linked glycans. These glycans are important pathogen associated molecular patterns (PAMPs) recognised by the innate immune system. Glycan synthesis is mediated by a series of glycosyl transferases, located in the endoplasmic reticulum and Golgi apparatus. Mnn2 is responsible for the addition of the initial α1,2-mannose residue onto the α1,6-mannose backbone, forming the N-mannan outer chain branches. In Candida albicans, the MNN2 gene family is comprised of six members (MNN2, MNN21, MNN22, MNN23, MNN24 and MNN26). Using a series of single, double, triple, quintuple and sextuple mutants, we show, for the first time, that addition of α1,2-mannose is required for stabilisation of the α1,6-mannose backbone and hence regulates mannan fibril length. Sequential deletion of members of the MNN2 gene family resulted in the synthesis of lower molecular weight, less complex and more uniform N-glycans, with the sextuple mutant displaying only un-substituted α1,6-mannose. TEM images confirmed that the sextuple mutant was completely devoid of the outer mannan fibril layer, while deletion of two MNN2 orthologues resulted in short mannan fibrils. These changes in cell wall architecture correlated with decreased proinflammatory cytokine induction from monocytes and a decrease in fungal virulence in two animal models. Therefore, α1,2-mannose of N-mannan is important for both immune recognition and virulence of C. albicans.
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“Cell wall and extracellular matrix polysaccharides have mechanistic roles implicated in the protection of Candida species from host response and drug therapies (13–16).”
From Dual function of Candida auris mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [14]
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“C. albicans has a well-characterized cell wall composed of an inner layer of chitin, β−1,3-glucan, and β−1,6-glucan, and an outer layer composed of proteins modified with N- and O-linked mannans and phosphomannans, called mannoproteins34,35.”
From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [34]
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Metadata
- Authors
- Hall, R. A., Bates, S., Lenardon, M. D., MacCallum, D. M., Wagener, J., Lowman, D. W., Kruppa, M. D., Williams, D. L., Odds, F. C., Brown, A. J. P., & Gow, N. A. R.
- Affiliations
- University of Aberdeen (GB)
- University of Exeter (GB)
- East Tennessee State University (US)
- Corresponding author
- Gow, Neil A. R.
- ORCID
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-04-25
- Volume
- 9
- Issue
- 4
- Pages
- e1003276
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC3636026
- OpenAlex
- W2086193922
- Cited by
- 128
- References
- 60
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 13 · 2023: 4 · 2022: 12 · 2021: 6 · 2020: 9 · 2019: 10 · 2018: 16 · 2017: 9 · 2016: 11 · 2015: 9 · 2014: 6 · 2013: 6
- FWCI
- 4.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Kent Academic Repository (University of Kent) (acceptedVersion)
- Aberdeen University Research Archive (Aberdeen University) (submittedVersion)
- Digital Commons - East Tennessee State University (East Tennessee State University) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Open Research Exeter (University of Exeter) (submittedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion, cc-by)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (099215, 086827, 080088, 075470)
- European Commission (260338)
- Medical Research Council (MR/J008230/1)
- Biotechnology and Biological Sciences Research Council (BB/F00513X/1)
- National Institute of General Medical Sciences (R01GM053522)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Keywords
- Candida albicans, fungal cell wall, glycosyltransferases, pathogen-associated molecular patterns, innate immune recognition, inflammatory cytokines, fungal virulence, GPI-anchored proteins, N-glycans
- MeSH terms
- Animals, Candida albicans, Candidiasis, Cell Wall, Female, Fungal Proteins, Humans, Mannans, Mannose, Mannosyltransferases, Membrane Glycoproteins, Mice, Inbred BALB C, Polysaccharides, Sequence Alignment, Sequence Deletion, Receptors, Pattern Recognition, Mice
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