| Summary: | Plant lectins are essentially carbohydrate-binding proteins that play crucial roles in various biological functions and activities. Pinellia ternata (Thunb.) Breit. is a well-known traditional herbal medicine with significant economic value. P. ternata agglutinin (PTA), a classic type of lectin, exhibits insecticidal, antimicrobial, and antiviral properties. In our study, we cloned nine full-length PTA genes. Bioinformatics analysis revealed that the PTA proteins contain conserved carbohydrate-binding domains and numerous phosphorylation sites, and they predominantly localize to the cell membrane and nucleus. Recombinant PTA proteins expressed in prokaryotic systems demonstrated species-specific hemagglutination activity, which can be inhibited by specific carbohydrates. Untargeted metabolomics analysis indicated that the overexpression of PTA5 and PTA6 in P. ternata callus significantly altered lipid and organic acid metabolism. Our findings provide a foundation for the application of P. ternata lectins in pharmaceutical development and crop improvement.
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