ThaumatinV1, Main, Exploration, bibRecord, 000523

Two antifungal thaumatin-like proteins from barley grain.

Identifieur interne : 000523 ( Main/Exploration ); précédent : 000522; suivant : 000524

Two antifungal thaumatin-like proteins from barley grain.

Auteurs : J. Hejgaard ; S. Jacobsen ; I. Svendsen

Source :

FEBS letters [ 0014-5793 ] ; 1991.

RBID : pubmed:1936240

Descripteurs français

KwdFr :
- Alignement de séquences (MeSH), Antifongiques (composition chimique), Antifongiques (isolement et purification), Antifongiques (pharmacologie), Données de séquences moléculaires (MeSH), Hordeum (composition chimique), Immunochimie (MeSH), Immunodiffusion (MeSH), Protéines végétales (composition chimique), Protéines végétales (isolement et purification), Protéines végétales (pharmacologie), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Antifongiques, Hordeum, Protéines végétales.
- isolement et purification : Antifongiques, Protéines végétales.
- pharmacologie : Antifongiques, Protéines végétales.
- Alignement de séquences, Données de séquences moléculaires, Immunochimie, Immunodiffusion, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Hordeum (chemistry), Immunochemistry (MeSH), Immunodiffusion (MeSH), Molecular Sequence Data (MeSH), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology), Sequence Alignment (MeSH).
MESH :
- chemical , chemistry : Antifungal Agents, Plant Proteins.
- chemical , isolation & purification : Antifungal Agents, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Plant Proteins.
- chemistry : Hordeum.
- Amino Acid Sequence, Immunochemistry, Immunodiffusion, Molecular Sequence Data, Sequence Alignment.

Abstract

Antifungal activity has been associated with 2 immunochemically distinct proteins, protein R and S (Mr approximately 23 kDa; pI 9-10), which were isolated in pure form from barley grain. The proteins are homologous with thaumatin- and pathogenesis-related proteins of the PR5 family. The proteins inhibit growth of i.a. Trichoderma viride and Candida albicans in microtiter plate assays and act synergistically with barley grain chitinase C. Like maize zeamatin, protein R and S but not chitinase C retarded fungal growth in synergism with nikkomycin Z, a nucleoside-peptide inhibitor of fungal chitin synthesis. Although no inhibition of alpha-amylases or serine proteases could be associated with protein R or S the results indicate that the homologous maize grain bifunctional inhibitor of insect alpha-amylase and trypsin is very similar to or identical with maize zeamatin, which was proposed to have permeabilizing activity towards fungal membranes. Thus, in addition to the intensely sweet properties of thaumatin, multiple unrelated defense functions against insect and fungal pests can now be associated with the family of thaumatin-homologous proteins.

DOI: 10.1016/0014-5793(91)81119-s
PubMed: 1936240

Affiliations:

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Le document en format XML

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<term>Antifungal Agents (pharmacology)</term>
<term>Hordeum (chemistry)</term>
<term>Immunochemistry (MeSH)</term>
<term>Immunodiffusion (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (isolation & purification)</term>
<term>Plant Proteins (pharmacology)</term>
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<term>Antifongiques (pharmacologie)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Hordeum (composition chimique)</term>
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<term>Immunodiffusion (MeSH)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (isolement et purification)</term>
<term>Protéines végétales (pharmacologie)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
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<term>Plant Proteins</term>
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<term>Protéines végétales</term>
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<front><div type="abstract" xml:lang="en">Antifungal activity has been associated with 2 immunochemically distinct proteins, protein R and S (Mr approximately 23 kDa; pI 9-10), which were isolated in pure form from barley grain. The proteins are homologous with thaumatin- and pathogenesis-related proteins of the PR5 family. The proteins inhibit growth of i.a. Trichoderma viride and Candida albicans in microtiter plate assays and act synergistically with barley grain chitinase C. Like maize zeamatin, protein R and S but not chitinase C retarded fungal growth in synergism with nikkomycin Z, a nucleoside-peptide inhibitor of fungal chitin synthesis. Although no inhibition of alpha-amylases or serine proteases could be associated with protein R or S the results indicate that the homologous maize grain bifunctional inhibitor of insect alpha-amylase and trypsin is very similar to or identical with maize zeamatin, which was proposed to have permeabilizing activity towards fungal membranes. Thus, in addition to the intensely sweet properties of thaumatin, multiple unrelated defense functions against insect and fungal pests can now be associated with the family of thaumatin-homologous proteins.</div>
</front>
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<Abstract><AbstractText>Antifungal activity has been associated with 2 immunochemically distinct proteins, protein R and S (Mr approximately 23 kDa; pI 9-10), which were isolated in pure form from barley grain. The proteins are homologous with thaumatin- and pathogenesis-related proteins of the PR5 family. The proteins inhibit growth of i.a. Trichoderma viride and Candida albicans in microtiter plate assays and act synergistically with barley grain chitinase C. Like maize zeamatin, protein R and S but not chitinase C retarded fungal growth in synergism with nikkomycin Z, a nucleoside-peptide inhibitor of fungal chitin synthesis. Although no inhibition of alpha-amylases or serine proteases could be associated with protein R or S the results indicate that the homologous maize grain bifunctional inhibitor of insect alpha-amylase and trypsin is very similar to or identical with maize zeamatin, which was proposed to have permeabilizing activity towards fungal membranes. Thus, in addition to the intensely sweet properties of thaumatin, multiple unrelated defense functions against insect and fungal pests can now be associated with the family of thaumatin-homologous proteins.</AbstractText>
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Two antifungal thaumatin-like proteins from barley grain.

Two antifungal thaumatin-like proteins from barley grain.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki