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Plant defense peptides
Author(s) -
GarcíaOlmedo Francisco,
Molina Antonio,
Alamillo Josefa M.,
RodríguezPalenzuéla Pablo
Publication year - 1998
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1998)47:6<479::aid-bip6>3.0.co;2-k
Subject(s) - chemistry , virulence , mutant , disulfide bond , pathogen , transgene , antimicrobial peptides , peptide , plant lipid transfer proteins , gene , human pathogen , virulence factor , cyclic peptide , plant defense against herbivory , biochemistry , computational biology , microbiology and biotechnology , biology
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