Cloning, expression and functional characterisation of a peroxiredoxin from the potato cyst nematode Globodera rostochiensis

• Published in: Molecular and biochemical parasitology 2000-11, Vol.111 (1), p.41-49
• Main Authors: Robertson, L, Robertson, W M, Sobczak, M, Helder, J, Tetaud, E, Ariyanayagam, M R, Ferguson, M A, Fairlamb, A, Jones, J T
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Blotting, Western; Brugia malayi; Cloning, Molecular; cumene; DNA, Helminth - genetics; Gene Library; Globodera rostochiensis; Hydrogen Peroxide - metabolism; Lycopersicon esculentum - parasitology; Molecular Sequence Data; Onchocerca volvulus; Peroxidases - chemistry; Peroxidases - genetics; Peroxidases - isolation & purification; Peroxidases - metabolism; peroxiredoxin; Peroxiredoxins; Plant Roots - parasitology; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Solanum tuberosum - parasitology; Substrate Specificity; t-butyl hydroperoxide; trypanothione; trypanothione reductase; tryparedoxin; Tylenchoidea - genetics; Tylenchoidea - physiology
• ISSN: 0166-6851
• DOI: 10.1016/S0166-6851(00)00295-4

We report the cloning, expression and functional characterisation of a peroxidase belonging to the peroxiredoxin family from the potato cyst nematode Globodera rostochiensis, the first molecule of this type from any nematode parasitic on plants. The G. rostochiensis peroxiredoxin catalyses the breakdown of hydrogen peroxide, but not cumene or t-butyl hydroperoxide, in a trypanosomatid reducing system comprising trypanothione reductase, trypanothione and tryparedoxin. In common with its homologues from Onchocerca volvulus and Brugia malayi, the G. rostochiensis enzyme is present on the surface of invasive and post-infective juveniles despite the apparent lack of a cleavable N-terminal signal peptide. The possibility that the G. rostochiensis peroxiredoxin plays a role in protection of the parasite from plant defence responses is discussed.