{"title":"蕨类植物中含有LysM结构域的几丁质酶:一种有前景的可持续生物农药资源。","authors":"M Annapoorneshwari, A Sharma, S Hegde","doi":"10.1111/plb.70093","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":220,"journal":{"name":"Plant Biology","volume":" ","pages":""},"PeriodicalIF":3.6000,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"LysM domain-containing chitinases in pteridophytes: A promising resource for sustainable biopesticides.\",\"authors\":\"M Annapoorneshwari, A Sharma, S Hegde\",\"doi\":\"10.1111/plb.70093\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":220,\"journal\":{\"name\":\"Plant Biology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":3.6000,\"publicationDate\":\"2025-08-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1111/plb.70093\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1111/plb.70093","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
LysM domain-containing chitinases in pteridophytes: A promising resource for sustainable biopesticides.
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.
期刊介绍:
Plant Biology is an international journal of broad scope bringing together the different subdisciplines, such as physiology, molecular biology, cell biology, development, genetics, systematics, ecology, evolution, ecophysiology, plant-microbe interactions, and mycology.
Plant Biology publishes original problem-oriented full-length research papers, short research papers, and review articles. Discussion of hot topics and provocative opinion articles are published under the heading Acute Views. From a multidisciplinary perspective, Plant Biology will provide a platform for publication, information and debate, encompassing all areas which fall within the scope of plant science.