Effects of a novel pathogenesis-related class 10 (PR-10) protein from Crotalaria pallida Roots with papain inhibitory activity against root-knot nematode Meloidogyne incognita
| Autor: | L. B. S. Andrade, Ilka M. Vasconcelos, Maurício P. Sales, Jannison K.C. Ribeiro, Jose Tadeu Abreu de Oliveira, Sumika Kiyota, Adeliana S. Oliveira |
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| Rok vydání: | 2010 |
| Předmět: |
Plant Roots
chemistry.chemical_compound Non-competitive inhibition Solanum lycopersicum Papain Meloidogyne incognita Root-knot nematode Animals Tylenchoidea Enzyme Inhibitors Peptide sequence Ammonium sulfate precipitation Plant Diseases Plant Proteins Gel electrophoresis biology General Chemistry biology.organism_classification Molecular Weight Kinetics Nematode Biochemistry chemistry Crotalaria General Agricultural and Biological Sciences |
| Zdroj: | Journal of agricultural and food chemistry. 58(7) |
| ISSN: | 1520-5118 |
| Popis: | A novel pathogenesis-related class 10 (PR-10) protein with papain inhibitory activity, named CpPRI, was purified from Crotalaria pallida roots by ammonium sulfate precipitation followed by three reverse-phase high-performance liquid chromatographies (HPLCs). CpPRI is made up of a single polypeptide chain with a M(r) of 15 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This protein exhibited a K(i) value of 1.8 x 10(-9) M and operates via a noncompetitive inhibition mechanism. The alignment of the N-terminal amino acid sequence of CpPRI with other proteins revealed its identity with PR-10 proteins. CpPRI acts against digestive proteinase from root-knot nematode Meloidogyne incognita and demonstrated nematostatic and nematicide effects on this parasite in bioassays. In a localization study, fluorescein-5-isothiocyanate (FITC)-CpPRI was observed to internalize and diffuse over the entire J2 body after 6 h of incubation. This fact could explain the natural tolerance of this plant species to nematodes. |
| Databáze: | OpenAIRE |
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