Onchocerca volvulus:Immunolocalization of the Extracellular CuZn Superoxide Dismutase Using Antibodies Raised against a 15-mer Epitope of This Enzyme

• Published in: Experimental parasitology Vol. 91; no. 1; pp. 1 - 6
• Main Authors: Wildenburg, Gabriele, Henkle-Dührsen, Kimberly
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 01-01-1999; Elsevier
• Subjects: Amino Acid Sequence; Animals; Antibody Specificity; Biochemistry. Physiology. Immunology. Molecular biology; Biological and medical sciences; Epithelial Cells - chemistry; Epithelial Cells - enzymology; Epitopes; Female; Ferric Compounds - analysis; Fundamental and applied biological sciences. Psychology; Hemosiderin - analysis; Immune Sera - immunology; Immunoenzyme Techniques; Intestines - chemistry; Intestines - enzymology; Invertebrates; Male; Molecular Sequence Data; Nemathelminthia. Plathelmintha; Onchocerca volvulus - chemistry; Onchocerca volvulus - enzymology; Physiology. Development; Superoxide Dismutase - analysis; Superoxide Dismutase - chemistry; Superoxide Dismutase - immunology; Uterus - enzymology; environmental oxidative stress; nematode; intestine; Onchocerca volvulus; Superoxide dismutase; iron; SOD2,Onchocerca volvulussuperoxide dismutase 2 (EC 1.15.1.1); secretory enzyme; Immunohistochemistry; Wall; Antigenic determinant; Enzyme; Antibody; Gut; Parasite; Extracellular; Uterus; Secretory protein; Helmintha; Epithelial cell; Nemathelminthia; Oxidoreductases; Invertebrata; Localization; Nematoda
• ISSN: 0014-4894; 1090-2449
• DOI: 10.1006/expr.1999.4352

Wildenburg, G., and Henkle-Dührsen, K. 1999.Onchocerca volvulus:Immunolocalization of the extracellular CuZn superoxide dismutase using antibodies raised against a 15-mer epitope of this enzyme.Experimental Parasitology91,1–6. The study describes the immuno-histological localization of the extracellular CuZn superoxide dismutase (SOD2) in the parasitic nematodeOnchocerca volvulus.Using specific antiserum raised against a 15-amino-acid peptide from the N-terminal region of the mature protein, this enzyme is detected primarily in the intestinal epithelium of the adult worms and to a lesser extent in the muscle cells of the uterine wall. A blocking experiment with the SOD2 peptide reduced the staining significantly, confirming specificity. The localization profile of SOD2 correlates extremely well with the localization of iron deposits in the gut and uterine muscle cells of adultO. volvulus.The detection of SOD2 in the functional intestine ofO. volvulus, together with the evidence that it is a secreted protein, indicates that this enzyme in parasitic nematodes is in a position to interact with host molecules. It also demonstrates the accessibility of the parasite enzyme to an inhibitor or blocking antibody.