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Chitinases are hydrolytic enzymes that catalyse the degradation of chitin, a major component of fungal cell walls and arthropod exoskeletons. Although extensively studied in higher plants, chitinases in pteridophytes remain largely unknown. This review examined the potential of pteridophyte chitinases as a promising resource for advanced biopesticides. Pteridophytes, including ferns and lycophytes, dating back over 450 million years, have evolved unique adaptations to terrestrial environments, suggesting they may possess novel chitinase variants. Research on fern chitinases, particularly in Pteris ryukyuensis and Equisetum arvense, has revealed distinct features, such as LysM domains, which enhance chitin-binding and antifungal activity. PrChi-A chitinase from P. ryukyuensis exhibits remarkable thermal stability and specific binding to chitin oligosaccharides, which could be advantageous for agricultural applications. Additionally, engineered multimeric LysM domains fused with catalytic domains have demonstrated enhanced antifungal effects compared to those of naturally occurring chitinases. These findings highlight the potential of pteridophyte chitinases in developing improved biopesticides against fungal pathogens. The unique evolutionary position of pteridophytes among non-vascular and seed plants suggests they may harbour additional novel chitinase variants with diverse biochemical properties. Further exploration of chitinases across various pteridophyte species could uncover enzymes with enhanced stability, specificity, and efficacy for sustainable agriculture and biotechnology. This review highlights the need for increased research on pteridophyte chitinases to harness their potential as valuable resources for cutting-edge biopesticides and other biotechnological applications.
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http://dx.doi.org/10.1111/plb.70093 | DOI Listing |
Plant Biol (Stuttg)
August 2025
Centre for Advanced Learning and Research, Mangaluru, Karnataka, India.
Chitinases are hydrolytic enzymes that catalyse the degradation of chitin, a major component of fungal cell walls and arthropod exoskeletons. Although extensively studied in higher plants, chitinases in pteridophytes remain largely unknown. This review examined the potential of pteridophyte chitinases as a promising resource for advanced biopesticides.
View Article and Find Full Text PDFPlant Sci
August 2022
Department of Advanced Bioscience, Kindai University, 3327-204, Nakamachi, Nara 631-8505, Japan. Electronic address:
A unique GH18 chitinase containing two N-terminal lysin motifs (PrLysM1 and PrLysM2) was first found in fern, Pteris ryukyuensis (Onaga and Taira, Glycobiology, 18, 414-423, 2008). This type of LysM-chitinase conjugates is not usually found in plants but in fungi. Here, we produced a similar GH18 chitinase with one N-terminal LysM module (EaLysM) from the fern, Equisetum arvense (EaChiA, Inamine et al.
View Article and Find Full Text PDFInt J Biol Macromol
July 2020
Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan; Department of Bioscience and Biotechnology, University of the Ryukyus, Okinawa, Japan. Electronic address:
PrChiA is an antifungal chitinase obtained from Pteris ryukyuensis, a fern plant. It consists of two N-terminal lysin motif (LysM) domains and a C-terminal catalytic domain of glycoside hydrolase family 18. Previous studies have shown that the deletion of LysM domains or loss of hydrolytic activity causes the loss of the antifungal activity of chitinases.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 2017
Department of Advanced Bioscience, Kindai University, 3327-204 Nakamachi, Nara 631-8505, Japan.
We determined the crystal structure of a LysM module from Pteris ryukyuensis chitinase-A (PrLysM2) at a resolution of 1.8 Å. Structural and binding analysis of PrLysM2 indicated that this module recognizes chitin oligosaccharides in a shallow groove comprised of five sugar-binding subsites on one side of the molecule.
View Article and Find Full Text PDFPlanta
October 2015
Department of Advanced Bioscience, Kinki University, 3327-204 Nakamachi, Nara, 631-8505, Japan.
We first solved the crystal structure of class III catalytic domain of a chitinase from fern (PrChiA-cat), and found a structural difference between PrChiA-cat and hevamine. PrChiA-cat was found to have reduced affinities to chitin oligosaccharides and allosamidin. Plant class III chitinases are subdivided into enzymes with three disulfide bonds and those without disulfide bonds.
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