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

78Citations
Citations of this article
25Readers
Mendeley users who have this article in their library.

Abstract

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 NiCl 2 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. © 1992.

Cite

CITATION STYLE

APA

Hejgaard, J., Jacobsen, S., Bjørn, S. E., & Kragh, K. M. (1992). Antifungal activity of chitin-binding PR-4 type proteins from barley grain and stressed leaf. FEBS Letters, 307(3), 389–392. https://doi.org/10.1016/0014-5793(92)80720-2

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free