{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:43:54Z","timestamp":1790520234344,"version":"4.1.0"},"reference-count":40,"publisher":"Wiley","issue":"20","license":[{"start":{"date-parts":[[2014,9,24]],"date-time":"2014-09-24T00:00:00Z","timestamp":1411516800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Russian Foundation for Basic Research","award":["12-04-00190-a"],"award-info":[{"award-number":["12-04-00190-a"]}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2014,10]]},"abstract":"<jats:p>The multilayered plant immune system relies on rapid recognition of pathogen\u2010associated molecular patterns followed by activation of defense\u2010related 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\u2010metalloproteinase from <jats:italic>Fusarium\u00a0verticillioides<\/jats:italic>, named fungalysin Fv\u2010cmp. This proteinase cleaves class\u00a0<jats:styled-content style=\"fixed-case\">IV<\/jats:styled-content> 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\u2010like antimicrobial peptides named wheat antimicrobial peptides (<jats:styled-content style=\"fixed-case\">WAMP<\/jats:styled-content>s) containing different amino acids (Ala, Lys, Glu, and Asn) at the nonconserved position\u00a034. An additional Ser at the site of fungalysin proteolysis makes the peptides resistant to the protease. Moreover, an equal molar concentration of <jats:styled-content style=\"fixed-case\">WAMP<\/jats:styled-content>\u20101b or <jats:styled-content style=\"fixed-case\">WAMP<\/jats:styled-content>\u20102 to chitinase was sufficient to block the fungalysin activity, keeping the chitinase intact. Thus, <jats:styled-content style=\"fixed-case\">WAMP<\/jats:styled-content>s represent novel protease inhibitors that are active against fungal metalloproteases. According to <jats:italic>in\u00a0vitro<\/jats:italic> antifungal assays <jats:styled-content style=\"fixed-case\">WAMP<\/jats:styled-content>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.<\/jats:p>","DOI":"10.1111\/febs.13015","type":"journal-article","created":{"date-parts":[[2014,8,23]],"date-time":"2014-08-23T11:38:58Z","timestamp":1408793938000},"page":"4754-4764","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":79,"title":["Novel mode of action of plant defense peptides\u00a0\u2013\u00a0hevein\u2010like antimicrobial peptides from wheat inhibit fungal metalloproteases"],"prefix":"10.1111","volume":"281","author":[{"given":"Anna A.","family":"Slavokhotova","sequence":"first","affiliation":[{"name":"Vavilov Institute of General Genetics Russian Academy of Sciences Moscow Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd A.","family":"Naumann","sequence":"additional","affiliation":[{"name":"Bacterial Foodborne Pathogens &amp; Mycology Research Unit USDA\u2010ARS\u2010NCAUR Peoria IL USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil P. 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