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Plant Defense Proteins: Recent Discoveries and Applications

DOE

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Proteins play pivotal roles in safeguarding plants against numerous biotic and abiotic stresses. Understanding their biological functions and mechanisms of action is essential for advancing plant biology, agriculture, and biotechnology. This review considers the diversity and potential applications of plant defense proteins including pathogenesis-related (PR) proteins, chitinases, glucanases, protease inhibitors, lectins, and antimicrobial peptides. Recent advances, such as the omics technologies, have enabled the discovery of new plant defense proteins and regulatory networks that govern plant defense responses and unveiled numerous roles of plant defense proteins in stress perception, signal transduction, and immune priming. The molecular affinities and enzymatic activities of plant defense proteins are essential for their defense functions. Applications of plant defense proteins span agriculture, biotechnology, and medicine, including the development of resistant crop varieties, bio-based products, biopharmaceuticals, and functional foods. Future research directions include elucidating the structural bases of defense protein functions, exploring protein interactions with ligands and other proteins, and engineering defense proteins for enhanced efficacy. Overall, this review illuminates the significance of plant defense proteins against biotic stresses in plant biology and biotechnology, emphasizing their potential for sustainable agriculture and environmental management.. Authors: Shobade, Samuel O. [Ames Lab., and Iowa State Univ., Ames, IA (United States)]; Nilsen-Hamilton, Marit [Ames Lab., and Iowa State Univ., Ames, IA (United States)] (ORCID:0000000254961814); Zabotina, Olga A. [Ames Lab., and Iowa State Univ., Ames, IA (United States)] (ORCID:0000000169386923). DOE Contract: AC02-07CH11358. Subjects: G-proteins; chitin-binding domain; chitinases; jacalin-related lectins; pathogenesis-related proteins; plant defense; rhizosphere; β-glucosidase

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