Design of self-processing antimicrobial peptides for plant protection
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Updated: Oct 13, 2026

Live-cell Imaging of Fungal Cells to Investigate Modes of Entry and Subcellular Localization of Antifungal Plant Defensins
Published on: December 24, 2017
W A Powell1, C M Catranis, C A Maynard
1SUNY, College of Environmental Science and Forestry, Syracuse, NY 13210-2788, USA. wapowell@mailbox.syr.edu
Abstract:
Small antimicrobial peptides are excellent candidates for inclusion in self-processing proteins that could be used to confer pathogen resistance in transgenic plants. Antimicrobial peptides as small as 22 amino acids in length have been designed to incorporate the residual amino acids left from protein processing by the tobacco etch virus'(TEVs') NIa protease. Also, by minimizing the length of these peptides and the number of highly hydrophobic residues, haemolytic activity was reduced without affecting the peptide's antimicrobial activity.
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