ArticleScientific reports2018
Structural insights into antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025Article
- Mycobiota and C-Type Lectin Receptors in Cancers: Know thy Neighbors.Frontiers in microbiology · 2022Review
- Article
- Mycobiome and Cancer: What Is the Evidence?Cancers · 2021Review
- Macrofungi as a Nutraceutical Source: Promising Bioactive Compounds and Market Value.Journal of fungi (Basel, Switzerland) · 2021Review
- 3D Structural Insights into β-Glucans and Their Binding Proteins.International journal of molecular sciences · 2021Review
- Bacteriome and mycobiome and bacteriome-mycobiome interactions in head and neck squamous cell carcinoma.Oncotarget · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Schizophyllan (SCH) is a high molecular weight homopolysaccharide composed of a β-(1,3)-D-glucan main chain with branching β-(1,6)-bound D-glucose residues. It forms triple helices that are highly stable towards heat and extreme pH, which provides SCH with interesting properties for industrial and medical applications. The recombinant anti-SCH antibody JoJ48C11 recognizes SCH and related β-(1,6)-branched β-(1,3)-D-glucans, but details governing its specificity are not known. Here, we fill this gap by determining crystal structures of the antigen binding fragment (Fab) of JoJ48C11 in the apo form and in complex with the unbranched β-(1,3)-D-glucose hexamer laminarihexaose 3.0 and 2.4 Å resolution, respectively. Together with docking studies, this allowed construction of a JoJ48C11/triple-helical SCH complex, leading to the identification of eight amino acid residues of JoJ48C11 (Tyr27
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Registered trials
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