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Resources » Paper

Liddell S et al. (1995) International C. elegans Meeting "EXTRACELLULAR AND CYTOPLASMIC Cu/Zn SUPEROXIDE DISMUTASES FROM HAEMONCHUS CONTORTUS, A NEMATODE PARASITE OF SHEEP"

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  • Comments on Liddell S et al. (1995) International C. elegans Meeting "EXTRACELLULAR AND CYTOPLASMIC Cu/Zn SUPEROXIDE DISMUTASES FROM HAEMONCHUS CONTORTUS, A NEMATODE PARASITE OF SHEEP" (0)

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00021908

    Liddell S, & Knox DP (1995). EXTRACELLULAR AND CYTOPLASMIC Cu/Zn SUPEROXIDE DISMUTASES FROM HAEMONCHUS CONTORTUS, A NEMATODE PARASITE OF SHEEP presented in International C. elegans Meeting. Unpublished information; cite only with author permission.

    Antioxidant enzymes are postulated to play an important role in parasite defence against the cellular, oxygen-mediated killing mechanisms of the host. In particular, recent reports of the presence of an extracellular form of the enzyme superoxide dismutase (SOD) in several parasitic helminths have fuelled speculations that secreted SODs contribute to parasite survival by acting as both antioxidants and as anti-inflammatory agents. We have isolated full length cDNAs encoding two forms of Cu/Zn SOD from the gastrointestinal ovine nematode H. contortus. The predicted amino acid sequences suggest that one class represents a cytoplasmic enzyme (SODc), whilst the other class (SODe) contains an additional 33 amino acids at the N-terminus with the characteristics of a signal sequence and therefore may represent an extracellular form of the enzyme. The deduced amino acid sequences share a higher degree of homology with the C. elegans SODs than with any other reported SOD sequences; SODc is 78% identical to SOD-1, and SODe is 62% identical to the second C. elegans Cu/Zn SOD (F55H2.1). All of the residues involved in catalysis, metal ion binding and intrachain di-sulphide bonding are conserved in the H. contortus SODs. The entire coding sequence of each cDNA was cloned into the E. coli expression vector pET22b(+). In the case of SODc, a soluble active enzyme was obtained. An antiserum raised against purified recombinant SODc reacted with two proteins with estimated molecular masses of 19.5 and 22 kDa on Western blots of extracts from adult parasites.


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