Fasciola hepatica: Heterologous Expression and Functional Characterization of a Thioredoxin Peroxidase

Salazar-Calderón, M., Martín-Alonso, J. M., Ruiz de Eguino, A. D., Casais, R., Marín, M. S., and Parra, F. 2000. Fasciola hepatica: Heterologous expression and functional characterization of a thioredoxin peroxidase. Experimental Parasitology95, 63–70. A Fasciola hepatica cDNA clone of 779 bp was is...

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Published in:	Experimental parasitology Vol. 95; no. 1; pp. 63 - 70
Main Authors:	Salazar-Calderón, Mara, Martín-Alonso, José M., Ruiz de Eguino, Arantxa D., Casais, Rosa, Marín, M.Soledad, Parra, Francisco
Format:	Journal Article
Language:	English
Published:	San Diego, CA Elsevier Inc 01-05-2000 Elsevier
Subjects:	Amino Acid Sequence Animals antioxidant protein Antioxidants - chemistry Antioxidants - isolation & purification Antioxidants - metabolism Base Sequence Biological and medical sciences Blotting, Northern Blotting, Southern Blotting, Western Cattle Cloning, Molecular DNA, Complementary - chemistry DNA, Helminth - chemistry Electrophoresis, Polyacrylamide Gel excretory–secretory extract (ESE) Fasciola hepatica Fasciola hepatica - enzymology Fasciola hepatica - genetics Fe3+/O2/thiol metal-catalyzed oxidation systems (MCO) Fundamental and applied biological sciences. Psychology Gene Expression glutamine synthase glutamine synthetase (GS) Host parasite relation; pathogenicity Invertebrates Molecular Sequence Data Nemathelminthia. Plathelmintha Neoplasm Proteins Open Reading Frames Peroxidases - chemistry Peroxidases - genetics Peroxidases - metabolism Peroxiredoxins Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA, Messenger - analysis Sequence Alignment Sequence Analysis, DNA Sequence Homology, Amino Acid Thioredoxin peroxidase thioredoxin peroxidase (TPx) TSA protein glutamine synthetase (GS) Fasciola hepatica TSA protein Fe3+/O2/thiol metal-catalyzed oxidation systems (MCO) antioxidant protein thioredoxin peroxidase (TPx) excretory–secretory extract (ESE) Host parasite relation Nucleotide sequence Enzyme Plathelmintha Parasite Antioxidant Gene expression Thioredoxin Trematoda Biological activity Peroxidases Complementary DNA Helmintha Peroxidase Oxidoreductases Recombinant protein Exocrine secretion Invertebrata Heterologous Aminoacid sequence
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Summary:	Salazar-Calderón, M., Martín-Alonso, J. M., Ruiz de Eguino, A. D., Casais, R., Marín, M. S., and Parra, F. 2000. Fasciola hepatica: Heterologous expression and functional characterization of a thioredoxin peroxidase. Experimental Parasitology95, 63–70. 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 (Mr 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 Fe3+/O2/DTT or Fe3+/O2/ascorbate metal-catalyzed oxidation systems.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0014-4894 1090-2449
DOI:	10.1006/expr.2000.4495