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Cited by 110Fungal and yeast genetics researchAntifungal resistance and susceptibilityFungal Infections and Studies

Scalar nanostructure of the Candida albicans cell wall; a molecular, cellular and ultrastructural analysis and interpretation

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Lenardon, Megan D., Sood, Prashant, Dorfmueller, Helge C., Brown, Alistair J.P., Gow, Neil A.R.·2020·The Cell Surface
DOI 10.1016/j.tcsw.2020.100047PMC PMC7691183
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Abstract

Despite the importance of fungal cell walls as the principle determinant of fungal morphology and the defining element determining fungal interactions with other cells, few scalar models have been developed that reconcile chemical and microscopic attributes of its structure. The cell wall of the fungal pathogen Candida albicans is comprised of an amorphous inner skeletal layer of β(1,3)- and β(1,6)-glucan and chitin and an outer fibrillar layer thought to be dominated by highly mannosylated cell wall proteins. The architecture of these two layers can be resolved at the electron microscopy level, but the visualised structure of the wall has not yet been defined precisely in chemical terms. We have therefore examined the precise structure, location and molecular sizes of the cell wall components using transmission electron microscopy and tomography and tested predictions of the cell wall models using mutants and agents that perturb the normal cell wall structure. We demonstrate that the fibrils are comprised of a frond of N-linked outer chain mannans linked to a basal layer of GPI-proteins concentrated in the mid-wall region and that the non-elastic chitin microfibrils are cantilevered with sufficient lengths of non-fibrillar chitin and/or β-glucan to enable the chitin-glucan cage to flex, e.g. during morphogenesis and osmotic swelling. We present the first three-dimensional nano-scalar model of the C. albicans cell wall which can be used to test hypotheses relating to the structure–function relationships that underpin the pathobiology of this fungal pathogen.

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  • These α-1,2-mannoses can be connected to the α-1,6-mannan backbone, as well as to β-1,2-mannose, α-1,3-mannose, and phosphate groups found in the sidechains.

    “These α-1,2-mannoses can be connected to the α-1,6-mannan backbone, as well as to β-1,2-mannose, α-1,3-mannose, and phosphate groups found in the sidechains27,35.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [27]

    The Introduction (page unavailable) describes an α(1,6)-mannose backbone with α- or β-mannoside side chains and says mannans can carry β(1,2)-phosphomannosides. The Results section on N-mannan fibrils (page unavailable) also places side branches on the α(1,6) backbone. Neither passage specifies α(1,2)-mannose connections to β(1,2)-mannose, α(1,3)-mannose, or phosphate groups as the claim does. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • The mannan components exhibited flexible motion, whether as long N-mannan fibrils extending through the outer layer or as shorter O-linked mannans associated with cell wall proteins in the inner region.

    “The mannan components exhibited flexible motion (Fig. 3e), whether as long N-mannan fibrils extending through the outer layer or as shorter O-linked mannans associated with cell wall proteins in the inner region27.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [27]

    The Results section identifies long N-mannan fibrils in the outer cell-wall layer, while the Introduction describes O-mannan as a short chain. The Discussion, under “Mannosylated cell wall proteins,” places mannosylated proteins in the inner layer and depicts their stalks with O-linked mannans. These passages support the structural description, but they do not establish flexible motion of either mannan component; page numbers are unavailable in our copy. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Cell wall adaptation to echinocandins is characterized by increased levels and exposure of chitin following depletion of a substantial portion of β-glucan.

    “These effects have been associated with cell wall adaptation to echinocandins, characterized by increased levels and exposure of chitin following the depletion of a substantial portion of β-glucan; however, our understanding of echinocandin-induced remodeling mechanism of Candida cell wall architecture remains limited24,27–29.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [27]

    The Results section describes chitin and β(1,3)-glucan in the cell wall and measures their levels in genetic mutants, not after echinocandin treatment. Searches for echinocandins, caspofungin, and compensatory chitin responses found no passage addressing increased chitin levels or exposure following drug-induced β-glucan depletion. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

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Authors
Lenardon, M. D., Sood, P., Dorfmueller, H. C., Brown, A. J. P., & Gow, N. A. R.
Affiliations
  • University of Aberdeen (GB)
  • University of Dundee (GB)
Corresponding author
  • Lenardon, Megan D.
  • Gow, Neil A.R.
ORCID
Venue
The Cell Surface
Publisher
Elsevier BV
Published
2020-12
Volume
6
Pages
100047
ISSN
2468-2330 (ISSN-L)
DOI
10.1016/j.tcsw.2020.100047
PMC
PMC7691183
OpenAlex
W3098453064
Cited by
110
References
10
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2026: 25 · 2025: 23 · 2024: 25 · 2023: 7 · 2022: 18 · 2021: 12
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journal article
Language
en
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Locations
  • The Cell Surface (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Discovery Research Portal (University of Dundee) (publishedVersion, cc-by)
  • Aberdeen University Research Archive (Aberdeen University) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • UNSWorks (University of New South Wales, Sydney, Australia) (submittedVersion, cc-by-nc-nd)
Funders
  • European Research Council (HEALTH-F2-2010-260338-ALLFUN)
  • Medical Research Council (MR/N006364/1, MR/J008230/1 MR/M026663/1)
  • Wellcome Trust (075470, 099197, 097377, 099215, 086827, 101873)
  • University of Aberdeen
  • University of New South Wales
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
  • Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
Keywords
Candida albicans, β-1,3-glucan, β-1,6-glucan, chitin microfibrils, GPI-anchored proteins, cell wall ultrastructure, cell wall mutants, osmotic swelling, morphogenesis, structure-function relationship

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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