Design of self-processing antimicrobial peptides for plant protection.
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.
Powell
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SUNY, College of Environmental Science and Forestry, Syracuse, NY 13210-2788, USA. wapowell@mailbox.syr.edu
Catranis
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CM
Maynard
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D016960:Agrobacterium tumefaciens / Q000187:drug effects; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology; D005670:Fusarium / Q000187:drug effects; D006461:Hemolysis; D006801:Humans; D054806:Magainins; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D010935:Plant Diseases / Q000382:microbiology*; D030821:Plants, Genetically Modified / Q000235:genetics*; D011549:Pseudomonas / Q000187:drug effects; D029867:Xenopus Proteins
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D010455:Peptides; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus