Structural highlights
Function
AMP_TRIKH Binds chitin. WAMP-1a has antifungal activity against the fungi F.solani (IC(50)=5 ug/ml), F.verticillioides (IC(50)=30 ug/ml), F.oxysporum (IC(50)=5 ug/ml), B.sorokiniana (IC(50)=5 ug/ml), B.cinerea (IC(50)=20 ug/ml) and N.crassa (IC(50)=10 ug/ml). Inhibits hyphal elongation and causes browning of hyphae in F.oxysporum. Causes destruction and discoloration of spores in B.sorokiniana. Inhibits the development of disease caused by the fungus P.infestans on potato tubers. Has antibacterial activity against the Gram-negative bacteria P.syringae and E.carotovora, and the Gram-positive bacterium C.michiganensis.[1]
Publication Abstract from PubMed
Hevein, a well-studied lectin from the rubber tree Hevea brasiliensis, is the title representative of a broad family of chitin-binding polypeptides. WAMP-1a, a peptide isolated from the wheat Triticum kiharae, shares considerable similarity with hevein. The peptide possesses antifungal, antibacterial activity and is thought to play an important role in the defense system of wheat. Importantly, it features a substitution of the conserved serine residue to glycine reducing its carbohydrate-binding capacity. We used NMR spectroscopy to derive the spatial structure of WAMP-1a in aqueous solution. Notably, the mutation was found to strengthen amphiphilicity of the molecule, associated with its mode of action, an indication of the hevein domain multi-functionality. Both primary and tertiary structure of WAMP-1a suggest its evolutionary origin from the hevein domain of plant chitinases.
Solution structure of a defense peptide from wheat with a 10-cysteine motif.,Dubovskii PV, Vassilevski AA, Slavokhotova AA, Odintsova TI, Grishin EV, Egorov TA, Arseniev AS Biochem Biophys Res Commun. 2011 Jul 22;411(1):14-8. Epub 2011 Jun 14. PMID:21704019[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA. A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif. FEBS J. 2009 Aug;276(15):4266-75. Epub 2009 Jul 3. PMID:19583772 doi:10.1111/j.1742-4658.2009.07135.x
- ↑ Dubovskii PV, Vassilevski AA, Slavokhotova AA, Odintsova TI, Grishin EV, Egorov TA, Arseniev AS. Solution structure of a defense peptide from wheat with a 10-cysteine motif. Biochem Biophys Res Commun. 2011 Jul 22;411(1):14-8. Epub 2011 Jun 14. PMID:21704019 doi:10.1016/j.bbrc.2011.06.058
