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Novel mode of action of plant defense peptides – hevein‐like antimicrobial peptides from wheat inhibit fungal metalloproteases
Author(s) -
Slavokhotova Anna A.,
Naumann Todd A.,
Price Neil P. J.,
Rogozhin Eugene A.,
Andreev Yaroslav A.,
Vassilevski Alexander A.,
Odintsova Tatyana I.
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13015
Subject(s) - chitinase , antimicrobial peptides , biology , protease , proteolysis , biochemistry , plant defense against herbivory , microbiology and biotechnology , antimicrobial , cell wall , metalloproteinase , mode of action , pathogen , enzyme , gene
The multilayered plant immune system relies on rapid recognition of pathogen‐associated molecular patterns followed by activation of defense‐related genes, resulting in the reinforcement of plant cell walls and the production of antimicrobial compounds. To suppress plant defense, fungi secrete effectors, including a recently discovered Zn‐metalloproteinase from Fusarium verticillioides , named fungalysin Fv‐cmp. This proteinase cleaves class IV chitinases, which are plant defense proteins that bind and degrade chitin of fungal cell walls. In this study, we investigated plant responses to such pathogen invasion, and discovered novel inhibitors of fungalysin. We produced several recombinant hevein‐like antimicrobial peptides named wheat antimicrobial peptides ( WAMP s) containing different amino acids (Ala, Lys, Glu, and Asn) at the nonconserved position 34. An additional Ser at the site of fungalysin proteolysis makes the peptides resistant to the protease. Moreover, an equal molar concentration of WAMP ‐1b or WAMP ‐2 to chitinase was sufficient to block the fungalysin activity, keeping the chitinase intact. Thus, WAMP s represent novel protease inhibitors that are active against fungal metalloproteases. According to in vitro antifungal assays WAMP s directly inhibited hyphal elongation, suggesting that fungalysin plays an important role in fungal development. A novel molecular mechanism of dynamic interplay between host defense molecules and fungal virulence factors is suggested.