Pathogen-induced proteins with inhibitory activity toward Phytophthora infestans
Autor: | Ben J. C. Cornelissen, J S Meulenhoff, Charles Peter Woloshuk, P.J.M. van den Elzen, Marianne Beatrix Sela-Buurlage |
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Rok vydání: | 1991 |
Předmět: |
Phytophthora
Hyphal growth Antifungal Agents Molecular Sequence Data Plant Science Biology Microbiology chemistry.chemical_compound Tobacco Plant defense against herbivory Tobacco mosaic virus Bioassay Amino Acid Sequence Peptide sequence Plant Diseases Plant Proteins chemistry.chemical_classification Sequence Homology Amino Acid Virulence fungi food and beverages Cell Biology Plants biology.organism_classification Immunity Innate Amino acid Tobacco Mosaic Virus Plants Toxic chemistry Phytophthora infestans Biological Assay Growth inhibition Research Article |
Zdroj: | The Plant Cell. 3:619-628 |
ISSN: | 1532-298X 1040-4651 |
DOI: | 10.1105/tpc.3.6.619 |
Popis: | A bioassay using Phytophthora infestans was developed to determine whether inhibitory proteins are induced in pathogen-inoculated plants. Using this bioassay, AP24, a 24-kilodalton protein causing lysis of sporangia and growth inhibition of P. infestans, was purified from tobacco plants inoculated with tobacco mosaic virus. Analysis of the N-terminal amino acid sequence identified AP24 as the thaumatin-like protein osmotin II. The sequence was also similar to NP24, the salt-induced protein from tomato. Subsequently, we purified a protein from tomato plants inoculated with P. infestans that had inhibitory activities identical to those of the tobacco AP24. The N-terminal amino acid sequence of this protein was also similar to those of osmotin and NP24. In general, both the tobacco and tomato AP24 caused lysis of sporangia at concentrations greater than 40 nanomolar and severely inhibited hyphal growth at concentrations greater than 400 nanomolar. Because both proteins were induced by pathogen inoculation, we discussed the possible involvement of these proteins as a plant defense mechanism. |
Databáze: | OpenAIRE |
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