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- Publisher
- Wiley
- Copyright
- Copyright © 1998 John Wiley & Sons, Inc.
- ISSN
- 0006-3525
- eISSN
- 1097-0282
- DOI
- 10.1002/(SICI)1097-0282(1998)47:6<479::AID-BIP6>3.0.CO;2-K
- pmid
- 10333739
- Publisher site
- See Article on Publisher Site
Abstract
Eight families of antimicrobial peptides, ranging in size from 2 to 9 kD, have been identified in plants. These are thionins, defensins, so‐called lipid transfer proteins, hevein‐ and knottin‐like peptides, MBP1, IbAMP, and the recently reported snakins. All of them have compact structures that are stabilized by 2–6 disulfide bridges. They are part of both permanent and inducible defense barriers. Transgenic overexpression of the corresponding genes leads to enhanced tolerance to pathogens, and peptide‐sensitive pathogen mutants have reduced virulence. © 1999 John Wiley & Sons, Inc. Biopoly 47: 479–491, 1998
Journal
Biopolymers – Wiley
Published: Jan 1, 1998