Purification and characterization of an antifungal thaumatin-like protein from Cassia didymobotrya cell culture.
Identifieur interne : 000379 ( Main/Curation ); précédent : 000378; suivant : 000380Purification 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. GiardinaSource :
- Plant physiology and biochemistry : PPB [ 0981-9428 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- 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
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pubmed:17056265Le 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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<keywords scheme="KwdFr" xml:lang="fr"><term>Antifongiques (métabolisme)</term>
<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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<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>
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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>
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