Katalog Plus
Bibliothek der Frankfurt UAS
Bald neuer Katalog: sichern Sie sich schon vorab Ihre persönlichen Merklisten im Nutzerkonto: Anleitung.
Dieses Ergebnis aus BASE kann Gästen nicht angezeigt werden.  Login für vollen Zugriff.

Gene expression and evolution of Bowman-Birk protease inhibitors in wild and domesticated Vigna (Fabaceae) species

Title: Gene expression and evolution of Bowman-Birk protease inhibitors in wild and domesticated Vigna (Fabaceae) species
Authors: Toini E.; Totaro M.; Silvestri G.; Vertemara J.; Zecca G.; Panzeri D.; Palm E. R.; Wagensommer R. P.; Zampella G.; Labra M.; Grassi F.
Contributors: Toini, E; Totaro, M; Silvestri, G; Vertemara, J; Zecca, G; Panzeri, D; Palm, E; Wagensommer, R; Zampella, G; Labra, M; Grassi, F
Publisher Information: Frontiers Media SA; CH
Publication Year: 2026
Collection: Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive)
Subject Terms: binding energy; bioprospecting; Bowman-Birk protease inhibitor; Fabaceae; gene diversity; Vigna
Description: Bowman-Birk protease inhibitors (BBIs) are multifunctional proteins with a double-headed structure, featuring two distinct inhibitory loops that target trypsin and chymotrypsin proteases. BBI regulates protease activity in plants and provides defense against pests and pathogens, but little is still known about their expression levels and their ability to interact with natural targets. Our results showed that BBI1 and BBI2 genes are the most highly expressed in Vigna seeds. Consequently, we produced two multiple sequence alignments including homologs from 42 Vigna taxa to explore variability and functionality. Phylogenetic relationships, signals of positive selection, and interaction energy levels with their natural targets were inferred. Overall, BBI2 exhibited the highest affinity for the assessed targets compared to BBI1. Amino acid substitutions have led to distinct protein variants across species, each displaying different interaction capacities with their respective targets. Additionally, the residue conferring inhibitory specificity for trypsin, located in the first domain, was found to be under positive selection in both genes. This suggests an ongoing evolutionary process aimed at optimizing affinity with proteases through continuous adaptation. Finally we emphasize that findings obtained can be used to drive the activity of plant breeders and more efficient cultivars can be selected. Given the growing availability of genomic information of wild and domesticated accessions, docking simulations offer a convenient and effective method to preliminarily assess new protein variants.
Document Type: article in journal/newspaper
File Description: ELETTRONICO
Language: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/41695539; info:eu-repo/semantics/altIdentifier/wos/WOS:001687325700001; volume:16; journal:FRONTIERS IN PLANT SCIENCE; https://hdl.handle.net/10281/596028
DOI: 10.3389/fpls.2025.1657741
Availability: https://hdl.handle.net/10281/596028; https://doi.org/10.3389/fpls.2025.1657741
Rights: info:eu-repo/semantics/openAccess ; license:Creative Commons ; license uri:http://creativecommons.org/licenses/by/4.0/
Accession Number: edsbas.C81D451
Database: BASE