Fasciola hepatica: heterologous expression and functional characterization of a thioredoxin peroxidase
| Autor: | José M. Martín-Alonso, Mara Salazar-Calderón, M. Soledad Marín, Rosa Casais, Arantxa D. Ruiz de Eguino, Francisco Parra |
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| Rok vydání: | 2000 |
| Předmět: |
DNA
Complementary Recombinant Fusion Proteins Immunology Blotting Western Molecular Sequence Data Gene Expression Biology medicine.disease_cause Antioxidants Open Reading Frames Complementary DNA Glutamine synthetase Gene expression medicine Animals Amino Acid Sequence RNA Messenger Cloning Molecular Escherichia coli Base Sequence Sequence Homology Amino Acid General Medicine Peroxiredoxins Sequence Analysis DNA DNA Helminth Fasciola hepatica Blotting Northern Molecular biology Fusion protein Neoplasm Proteins Open reading frame Blotting Southern Infectious Diseases Biochemistry Peroxidases Parasitology Cattle Electrophoresis Polyacrylamide Gel Heterologous expression Thioredoxin Sequence Alignment |
| Zdroj: | Experimental parasitology. 95(1) |
| ISSN: | 0014-4894 |
| Popis: | A Fasciola hepatica cDNA clone of 779 bp was isolated from an adult worm cDNA expression library by immunological screening using a rabbit serum against the excretory-secretory antigens. The nucleotide sequence of the cDNA revealed the presence of an open reading frame of 582 bp which encoded a 194-amino-acid-residue polypeptide (M(r) 21,723 Da) showing a high degree of homology to thioredoxin peroxidases. This putative antioxidant protein gene was expressed in Escherichia coli as a GST fusion protein. The recombinant fusion protein showed in vitro antioxidant properties and protected rabbit muscle enolase and E. coli glutamine synthetase from inactivation by nonenzymatic Fe(3+)/O(2)/DTT or Fe(3+)/O(2)/ascorbate metal-catalyzed oxidation systems. |
| Databáze: | OpenAIRE |
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