Heterologous expression and functional characterization of thioredoxin from Fasciola hepatica.
The full thioredoxin coding sequence from Fasciola hepatica has been cloned into the pGEX-2T expression vector and produced in Escherichia coli as a fusion protein. The recombinant protein proved to be biologically active, using an insulin reduction assay, and was also able to activate thioredoxin peroxidase from F. hepatica. These observations suggest that this protein could participate in a redox cascade involved in the maintenance of cell homeostasis as well as in parasite protection against reactive oxygen species produced by the host.
Salazar-Calderón
M
M
Departamento de Bioquímica & Biología Molecular, Universidad de Oviedo, Spain.
Martín-Alonso
J M
JM
Ruiz de Eguino
A D
AD
Parra
F
F
D000595:Amino Acid Sequence; D000818:Animals; D000975:Antioxidants / Q000494:pharmacology; D015152:Blotting, Northern; D018509:DNA, Helminth / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005210:Fasciola hepatica / Q000378:metabolism*; D018014:Gene Transfer Techniques; D005822:Genetic Vectors; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors / Q000378:metabolism; D015151:Immunoblotting; D007328:Insulin / Q000378:metabolism; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D010084:Oxidation-Reduction / Q000187:drug effects; D010544:Peroxidases / Q000378:metabolism; D054464:Peroxiredoxins; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000378:metabolism / Q000494:pharmacology; D016415:Sequence Alignment; D013879:Thioredoxins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology
D000975:Antioxidants; D018509:DNA, Helminth; D007328:Insulin; D009363:Neoplasm Proteins; D011993:Recombinant Fusion Proteins; D013879:Thioredoxins; D010544:Peroxidases; D054464:Peroxiredoxins; D005974:Glutamate-Ammonia Ligase