Antifungal activity of chitin‐binding PR‐4 type proteins from barley grain and stressed leaf

FEBS Letters

Kragh, Karsten M.²  Bjørn, Søren E.¹  Jacobsen, Susanne¹  Hejgaard, Jørn¹ 

[1] Department of Biochemistry and Nutrition, Bldg 224, Technical University of Denmark, DK-2800 Lyngby, Denmark;Maribo Seed, Biotechnology, PO Box 17, DK-1001 Copenhagen K, Denmark

关键词: Amino acid sequence;    Antifungal;    Hevein;    Pathogenesis related;    Win protein;    Hordeum vulgare;    CB;    chitin binding;    IWF;    intercellular washing fluid;    PDMS;    plasma desorption mass spectrometry;    PR;    pathogenesis related;    RP-HPLC;    reversed-phase high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(92)80720-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Antifungal activity in vitro has been associated with barley leaf and grain proteins which are homologous with pathogenesis related proteins of type 4 (PR-4) from tobacco and tomato and with C terminal domains of potato win and Hevea hevein precursor proteins. One protein (pI ∼9.3, M _r ∼13.7 kDa) from barley grain and two very similar proteins from leaves infected with Erysiphe graminis were isolated by chitin affinity chromatography, but none of the proteins showed chitinase activity in vitro. The leaf proteins were increased several fold in response to either Erysiphe infection or NiCl₂ infiltration and accumulated extracellularly. The three barley proteins were found to inhibit growth of Trichoderma harzianum in microtiter plate assays using ∼-10 μg/ml concentrations and in lower concentrations in a synergistic way when mixed either with barley chitinase C (a PR-3 type protein) or with barley protein R (a PR-5 type protein). Structurally similar proteins were detected in wheat, rye and oats grain extracts.

【 授权许可】

Unknown