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Cited by 57Polysaccharides and Plant Cell WallsImmune Response and InflammationGlycosylation and Glycoproteins Research

3D Structural Insights into β-Glucans and Their Binding Proteins

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Manabe, Noriyoshi, Yamaguchi, Yoshiki·2021·International Journal of Molecular Sciences
DOI 10.3390/ijms22041578PMC PMC7915573
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Abstract

β(1,3)-glucans are a component of fungal and plant cell walls. The β-glucan of pathogens is recognized as a non-self-component in the host defense system. Long β-glucan chains are capable of forming a triple helix structure, and the tertiary structure may profoundly affect the interaction with β-glucan-binding proteins. Although the atomic details of β-glucan binding and signaling of cognate receptors remain mostly unclear, X-ray crystallography and NMR analyses have revealed some aspects of β-glucan structure and interaction. Here, we will review three-dimensional (3D) structural characteristics of β-glucans and the modes of interaction with β-glucan-binding proteins.

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  • C. albicans cell walls share a relatively simple structure, with the rigid structural framework containing only chitin microfibrils and stiff linear β-1,3-glucan backbones, which may primarily adopt the triple helix conformation, within the inner layer.

    “These findings demonstrate that C. albicans cell walls share a relatively simple structure, with the rigid structural framework containing only chitin microfibrils and stiff linear β-1,3-glucan backbones, which may primarily adopt the triple helix conformation67–69, within the inner layer.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [67]

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  • Among these two forms, the former corresponds to type-a β-1,3-glucan observed at room-temperature, representing the bulk β-1,3-glucans in the model triple-helix configuration, exhibiting no interaction with chitin.

    “Among these two forms, the former corresponds to type-a β-1,3-glucan observed at room-temperature (Fig. 2e), representing the bulk β-1,3-glucans in the model triple-helix configuration67–69, exhibiting no interaction with chitin.”

    From Distinct echinocandin responses of Candida albicans and Candida auris cell walls revealed by solid-state NMR (2025) · cites this paper as [67]

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Authors
Manabe, N., & Yamaguchi, Y.
Affiliations
Tohoku Medical and Pharmaceutical University (JP)
Corresponding author
Yamaguchi, Yoshiki
ORCID
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-02-04
Volume
22
Issue
4
Pages
1578
ISSN
1422-0067 (ISSN-L)
DOI
10.3390/ijms22041578
PMC
PMC7915573
OpenAlex
W3129123925
Cited by
57
References
0
Citations by year
2026: 20 · 2025: 17 · 2024: 6 · 2023: 6 · 2022: 6 · 2021: 2
FWCI
0.48
Type
journal article
Language
en
Open access
Licence
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
KAKENHI (16H04758, 19H03362)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Polysaccharides and Plant Cell Walls
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
β-1,3-glucan, fungal cell wall, plant cell wall, triple helix, host defense, pattern recognition receptors, protein-ligand interactions, fungal pathogens
MeSH terms
Animals, Binding Sites, Carrier Proteins, Humans, Models, Molecular, Protein Binding, Crystallography, X-Ray, Lectins, beta-Glucans

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