Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties
- Author
- Xiaochen Wang, Guy Bauw (UGent) , Els Van Damme (UGent) , Willy J Peumans, Zhang-Liang Chen, Marc Van Montagu (UGent) , Geert Angenon (UGent) and Willy Dillen (UGent)
- Organization
- Abstract
- The orchid Gastrodia elata depends on the fungus Armillaria mellea to complete its life cycle. In the interaction, fungal hyphae penetrate older, nutritive corms but not newly formed corms. From these corms, a protein fraction with in vitro activity against plant-pathogenic fungi has previously been purified. Here, the sequence of gastrodianin, the main constituent of the antifungal fraction, is reported. Four isoforms that encoded two different mature proteins were identified at the cDNA level. Another isoform was detected in sequenced peptides. Because the antifungal activity of gastrodianins produced in and purified from Escherichia coil and Nicotiana tabacum was comparable to that of gastrodianin purified from the orchid, gastrodianins are the active component of the antifungal fractions. Gastrodianin accumulation is probably an important part of the mechanism by which the orchid controls Armillaria penetration. Gastrodianin was found to be homologous to monomeric mannose-binding proteins of other orchids, of which at least one (Epipactis helleborine mannose-binding protein) also displayed in vitro antifungal activity. This establishes the gastrodianin-like proteins (GLIPs) as a novel class of antifungal proteins.
- Keywords
- MIRABILIS-JALAPA, EPIPACTIS-HELLEBORINE, ESCHERICHIA-COLI, ACTIN-BINDING, FUNGAL GROWTH, ENHANCED RESISTANCE, ANTIMICROBIAL PEPTIDES, MOLECULAR-CLONING, SPECIES LISTERA-OVATA, TRANSGENIC TOBACCO PLANTS, Orchidaceae, mannose-binding protein, lectin, Gastrodia elata, antifungal protein, Epipactis helleborine
Downloads
-
(...).pdf
- full text
- |
- UGent only
- |
- |
- 283.33 KB
Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-168738
- MLA
- Wang, Xiaochen, Guy Bauw, Els Van Damme, et al. “Gastrodianin-like Mannose-binding Proteins: a Novel Class of Plant Proteins with Antifungal Properties.” PLANT JOURNAL 25.6 (2001): 651–661. Print.
- APA
- Wang, Xiaochen, Bauw, G., Van Damme, E., Peumans, W. J., Chen, Z.-L., Van Montagu, M., Angenon, G., et al. (2001). Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties. PLANT JOURNAL, 25(6), 651–661.
- Chicago author-date
- Wang, Xiaochen, Guy Bauw, Els Van Damme, Willy J Peumans, Zhang-Liang Chen, Marc Van Montagu, Geert Angenon, and Willy Dillen. 2001. “Gastrodianin-like Mannose-binding Proteins: a Novel Class of Plant Proteins with Antifungal Properties.” Plant Journal 25 (6): 651–661.
- Chicago author-date (all authors)
- Wang, Xiaochen, Guy Bauw, Els Van Damme, Willy J Peumans, Zhang-Liang Chen, Marc Van Montagu, Geert Angenon, and Willy Dillen. 2001. “Gastrodianin-like Mannose-binding Proteins: a Novel Class of Plant Proteins with Antifungal Properties.” Plant Journal 25 (6): 651–661.
- Vancouver
- 1.Wang X, Bauw G, Van Damme E, Peumans WJ, Chen Z-L, Van Montagu M, et al. Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties. PLANT JOURNAL. 2001;25(6):651–61.
- IEEE
- [1]X. Wang et al., “Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties,” PLANT JOURNAL, vol. 25, no. 6, pp. 651–661, 2001.
@article{168738,
abstract = {The orchid Gastrodia elata depends on the fungus Armillaria mellea to complete its life cycle. In the interaction, fungal hyphae penetrate older, nutritive corms but not newly formed corms. From these corms, a protein fraction with in vitro activity against plant-pathogenic fungi has previously been purified. Here, the sequence of gastrodianin, the main constituent of the antifungal fraction, is reported. Four isoforms that encoded two different mature proteins were identified at the cDNA level. Another isoform was detected in sequenced peptides. Because the antifungal activity of gastrodianins produced in and purified from Escherichia coil and Nicotiana tabacum was comparable to that of gastrodianin purified from the orchid, gastrodianins are the active component of the antifungal fractions. Gastrodianin accumulation is probably an important part of the mechanism by which the orchid controls Armillaria penetration. Gastrodianin was found to be homologous to monomeric mannose-binding proteins of other orchids, of which at least one (Epipactis helleborine mannose-binding protein) also displayed in vitro antifungal activity. This establishes the gastrodianin-like proteins (GLIPs) as a novel class of antifungal proteins.},
author = {Wang, Xiaochen and Bauw, Guy and Van Damme, Els and Peumans, Willy J and Chen, Zhang-Liang and Van Montagu, Marc and Angenon, Geert and Dillen, Willy},
issn = {0960-7412},
journal = {PLANT JOURNAL},
keywords = {MIRABILIS-JALAPA,EPIPACTIS-HELLEBORINE,ESCHERICHIA-COLI,ACTIN-BINDING,FUNGAL GROWTH,ENHANCED RESISTANCE,ANTIMICROBIAL PEPTIDES,MOLECULAR-CLONING,SPECIES LISTERA-OVATA,TRANSGENIC TOBACCO PLANTS,Orchidaceae,mannose-binding protein,lectin,Gastrodia elata,antifungal protein,Epipactis helleborine},
language = {eng},
number = {6},
pages = {651--661},
title = {Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties},
url = {http://dx.doi.org/10.1046/j.1365-313x.2001.00999.x},
volume = {25},
year = {2001},
}
- Altmetric
- View in Altmetric
- Web of Science
- Times cited: