ArticlePlanta2023
Characterization of an antifungal β-1,3-glucanase from Ficus microcarpa latex and comparison of plant and bacterial β-1,3-glucanases for fungal cell wall β-glucan degradation.
Article in Planta, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.
- The combined use of residual network and meta-analysis for pre-harvest diagnosis of kiwifruit gray mold disease and screening of efficient post-harvest control measures.Pest management science · 2026Pooled it
- A β-1,3-glucanase antagonizes a phase-separating WRKY repressor to confer saline-alkaline tolerance in rice.The New phytologist · 2026Article
- Effect of Supplementing Exogenous Glucanase or/and Mannanase to Diets Containing Torula Yeast on Growth Performance, Biochemical Indices, Liver and Intestinal Morphology, and Intestinal Microbiota and Metabolism of Largemouth Bass (Micropterus salmoides).Probiotics and antimicrobial proteins · 2026Article
- Metagenomic and physicochemical profiling reveal microbial functions in pit mud for Jiang-Nong Jianxiang Baijiu fermentation.BMC microbiology · 2025Article
- Antifungal characterizations of a novel endo-β-1,6-glucanase from Flavobacterium sp. NAU1659.Applied microbiology and biotechnology · 2024Article
- Glyoxal oxidase-mediated detoxification of reactive carbonyl species contributes to virulence, stress tolerance, and development in a pathogenic fungus.PLoS pathogens · 2024Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MAIN
conclusionEach β-1,3-glucanase with antifungal activity or yeast lytic activity hydrolyzes different structures of β-1,3-glucans in the fungal cell wall, respectively. Plants express several glycoside hydrolases that target chitin and β-glucan in fungal cell walls and inhibit pathogenic fungal infection. An antifungal β-1,3-glucanase was purified from gazyumaru (Ficus microcarpa) latex, designated as GlxGluA, and the corresponding gene was cloned and expressed in Escherichia coli. The sequence shows that GlxGluA belongs to glycoside hydrolase family 17 (GH17). To investigate how GlxGluA acts to degrade fungal cell wall β-glucan, it was compared with β-1,3-glucanase with different substrate specificities. We obtained recombinant β-1,3-glucanase (designated as CcGluA), which belongs to GH64, from the bacterium Cellulosimicrobium cellulans. GlxGluA inhibited the growth of the filamentous fungus Trichoderma viride but was unable to lyse the yeast Saccharomyces cerevisiae. In contrast, CcGluA lysed yeast cells but had a negligible inhibitory effect on the growth of filamentous fungi. GlxGluA degraded the cell wall of T. viride better than CcGluA, whereas CcGluA degraded the cell wall of S. cerevisiae more efficiently than GlxGluA. These results suggest that the target substrates in fungal cell walls differ between GlxGluA (GH17 class I β-1,3-glucanase) and CcGluA (GH64 β-1,3-glucanase).
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Registered trials
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