ThaumatinV1, Main, Exploration, bibRecord, 000382

Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture.

Identifieur interne : 000382 ( Main/Exploration ); précédent : 000381; suivant : 000383

Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture.

Auteurs : A. Vitali [Italie] ; L. Pacini ; E. Bordi ; P. De Mori ; L. Pucillo ; B. Maras ; B. Botta ; A. Brancaccio ; B. Giardina

Source :

Plant physiology and biochemistry : PPB [ 0981-9428 ] ; 2006.

RBID : pubmed:17056265

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (metabolism), Cassia (metabolism), Cells, Cultured (MeSH), Gene Expression Regulation, Plant (MeSH), Molecular Sequence Data (MeSH), Plant Proteins (metabolism).
MESH :
- chemical , metabolism : Antifungal Agents, Plant Proteins.
- metabolism : Cassia.
- Amino Acid Sequence, Cells, Cultured, Gene Expression Regulation, Plant, Molecular Sequence Data.

Abstract

A 23-kDa antifungal thaumatin-like protein was isolated and purified from Cassia didymobotrya (Fres.) cell cultures for the first time. The protein was secreted in the culture medium, but it could be also isolated after elution of whole cells with a 0.5 M CaCl(2) solution. Treatment of the cells with laminarin oligosaccharides or salicylic acid, but not with NaCl, resulted in enhancement of expression of the protein. A rapid purification protocol was used based on cationic exchange chromatography. The protein, with a highly basic character (pI 10), has an exact molecular mass of 23034 Da, as determined by MALDI-ToF mass spectrometry analysis. N-terminal sequencing of the intact polypeptide and the sequencing of two internal tryptic peptides indicated significant identity with other thaumatin-like proteins (TLP). The protein exerted antifungal activity towards some Candida species showing EC(50) values comparable to those of other antifungal TLPs. The collected data lead to classify this TLP as a new PR-5 protein.

DOI: 10.1016/j.plaphy.2006.09.008
PubMed: 17056265

Affiliations:

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Le document en format XML

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<term>Cells, Cultured (MeSH)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plant Proteins (metabolism)</term>
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<term>Cassia (métabolisme)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Plant Proteins</term>
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<term>Gene Expression Regulation, Plant</term>
<term>Molecular Sequence Data</term>
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<term>Données de séquences moléculaires</term>
<term>Régulation de l'expression des gènes végétaux</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">A 23-kDa antifungal thaumatin-like protein was isolated and purified from Cassia didymobotrya (Fres.) cell cultures for the first time. The protein was secreted in the culture medium, but it could be also isolated after elution of whole cells with a 0.5 M CaCl(2) solution. Treatment of the cells with laminarin oligosaccharides or salicylic acid, but not with NaCl, resulted in enhancement of expression of the protein. A rapid purification protocol was used based on cationic exchange chromatography. The protein, with a highly basic character (pI 10), has an exact molecular mass of 23034 Da, as determined by MALDI-ToF mass spectrometry analysis. N-terminal sequencing of the intact polypeptide and the sequencing of two internal tryptic peptides indicated significant identity with other thaumatin-like proteins (TLP). The protein exerted antifungal activity towards some Candida species showing EC(50) values comparable to those of other antifungal TLPs. The collected data lead to classify this TLP as a new PR-5 protein.</div>
</front>
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<DateCompleted><Year>2007</Year>
<Month>02</Month>
<Day>01</Day>
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<DateRevised><Year>2020</Year>
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<Abstract><AbstractText>A 23-kDa antifungal thaumatin-like protein was isolated and purified from Cassia didymobotrya (Fres.) cell cultures for the first time. The protein was secreted in the culture medium, but it could be also isolated after elution of whole cells with a 0.5 M CaCl(2) solution. Treatment of the cells with laminarin oligosaccharides or salicylic acid, but not with NaCl, resulted in enhancement of expression of the protein. A rapid purification protocol was used based on cationic exchange chromatography. The protein, with a highly basic character (pI 10), has an exact molecular mass of 23034 Da, as determined by MALDI-ToF mass spectrometry analysis. N-terminal sequencing of the intact polypeptide and the sequencing of two internal tryptic peptides indicated significant identity with other thaumatin-like proteins (TLP). The protein exerted antifungal activity towards some Candida species showing EC(50) values comparable to those of other antifungal TLPs. The collected data lead to classify this TLP as a new PR-5 protein.</AbstractText>
</Abstract>
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<ForeName>A</ForeName>
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Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture.

Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture.

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