Abstract
Peptide fragments that exhibit antimicrobial activity in vitro have been shown to be produced by cleavage from the hydrophilic region near the N terminus of various vicilin proteins in plant seeds. Three peptide sequences identified in the hydrophilic region of vicilin seed proteins of Macadamia integrifolia and Theobroma cacao were predicted to exhibit antimicrobial activity based on sequence similarity to antimicrobial peptides that had been previously purified from macadamia kernels. Histidine-tagged versions of the putative antimicrobial peptides were expressed in Escherichia coli, purified, and demonstrated to have in vitro antimicrobial activity. There are many vicilin sequences in the growing plant genome sequence databases, and this expression method provides a high-throughput process for functionally testing the potential of internal peptide fragments of vicilins as novel antimicrobial molecules.
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Acknowledgment
We are grateful to J. Green, A. M. Plume, A. Rusu, and N. Willemsen for technical assistance.
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Marcus, J.P., Goulter, K.C. & Manners, J.M. Peptide Fragments From Plant Vicilins Expressed in Escherichia Coli Exhibit Antimicrobial Activity In Vitro . Plant Mol Biol Rep 26, 75–87 (2008). https://doi.org/10.1007/s11105-008-0024-9
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DOI: https://doi.org/10.1007/s11105-008-0024-9