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zeamatin/zea mays

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Characterization and expression of an antifungal zeamatin-like protein (Zlp) gene from Zea mays.

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A cDNA clone encoding a basic thaumatin-like protein of Zea mays was recovered from a mid-development seed cDNA library. The gene, Zlp, encoded a protein that was nearly identical with maize zeamatin and alpha-amylase/trypsin inhibitor. Expression of Zlp mRNA was highest in the endosperm tissue of

Zeamatin inhibits trypsin and alpha-amylase activities.

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Zeamatin is a 22-kDa protein isolated from Zea mays that has antifungal activity against human and plant pathogens. Unlike other pathogenesis-related group 5 proteins, zeamatin inhibits insect alpha-amylase and mammalian trypsin activities. It is of clinical significance that zeamatin did not

Pilot-scale purification of zeamatin, an antifungal protein from maize.

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Zeamatin is an antifungal protein isolated from the seeds of Zea mays. A practical process for isolation and purification was developed to increase recovery yields for future testing of zeamatin as a novel therapeutic drug. Zeamatin was extracted with buffer from corn meal milled to flour. Solids

Antifungal-protein production in maize (Zea mays) suspension cultures.

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The growing emergency due to the phenomenon of drug resistance to micro-organisms has pushed forward the search for new potential drug alternatives to those already in use. Plants represent a suitable source of new antifungal molecules, as they produce a series of defensive proteins. Among them are

Several thaumatin-like proteins bind to beta-1,3-glucans.

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Pathogenesis-related proteins from intercellular fluid washings of stressed barley (Hordeum vulgare L.) leaves were analyzed to determine their binding to various water-insoluble polysaccharides. Three proteins (19, 16, and 15 kD) bound specifically to several water-insoluble beta-1,3-glucans.

Expression of a plant protein by Neurospora crassa.

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Heterologous expression of plant genes may serve as an important alternative for producing plant proteins. We have investigated the ability of the fungus Neurospora crassa to secrete zeamatin, a protein produced by Zea mays. Zeamatin was induced after being fused to glucoamylase, an extracellular

TLXI, a novel type of xylanase inhibitor from wheat (Triticum aestivum) belonging to the thaumatin family.

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Wheat (Triticum aestivum) contains a previously unknown type of xylanase (EC 3.2.1.8) inhibitor, which is described in the present paper for the first time. Based on its >60% similarity to TLPs (thaumatin-like proteins) and the fact that it contains the Prosite PS00316 thaumatin family signature, it
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