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Characterization of peptidases of adult Trichuris muris

Published online by Cambridge University Press:  06 April 2009

L. J. Drake ,
A. E. Bianco ,
D. A. P. Bundy  and
F. Ashall
L. J. Drake
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
A. E. Bianco
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
D. A. P. Bundy
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
F. Ashall
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
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Extract

Excretory/secretory (E/S) material of Trichuris muris was found to contain 2 major peptidases, Mr 85 and 105 kDa, which degrade gelatin optimally at pH 6·0 in sodium dodecyl sulphate–polyacrylamide gels. The peptidases were inactivated diisopropylfluorophosphate, leupeptin and soybean trypsin inhibitor, but were unaffected by inhibitors of aspartic-, cysteine- and metallo-peptidases, indicating that they are serine peptidases. Both enzymes were detectable within 5 h after incubation of worms in culture medium and showed a time-dependent increase in levels. Neither peptidase was detected in worm extracts, suggesting that they are activated during or following secretion from worms. Live worms degraded radio-isotope labelled extracellular matrix protein substratum derived from mammalian cells. Aminopeptidase activities capable of catalysing hydrolysis of amino acyl aminomethylcoumarin (MCA) substrates and a Z-Phe-Arg-MCA-hydrolysing cysteine peptidase activity, were detected in extracts of adult worms but not in E/S material.

Keywords

peptidaseTrichuris murisexcretory/secretory materialserine peptidase
Type
Research Article
Information
Parasitology , Volume 109 , Issue 5 , December 1994 , pp. 623 - 630
Copyright
Copyright © Cambridge University Press 1994

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References

REFERENCES

Ashall, F., Harris, H., Healy, N. & Shaw, E. (1990). Substrate specificity and inhibitor sensitivity of a trypanosomatid alkaline peptidase. Biochimica et Biophysica Acta 1035, 293–9.CrossRefGoogle ScholarPubMed
Barrett, A. J. & Kirschke, H. (1981). Cathepsins B and L. Methods in Enzymology 80, 536–41.Google Scholar
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Annals of Biochemistry 72, 248–54.CrossRefGoogle ScholarPubMed
Braun-Breton, C., Rosenberry, T. L. & Da Silva, L. P. (1988). Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C. Nature, London 332, 457–9.CrossRefGoogle ScholarPubMed
Bundy, D. A. P. & Cooper, E. S. (1989). Trichuris and trichuriasis in humans. Advances in Parasitology 28, 107–73.CrossRefGoogle ScholarPubMed
Chappell, C. L. & Dresden, M. H. (1986). Schistosoma mansoni: protease activity of haemoglobinase from the digestive tract of adult worms. Experimental Parasitology 61, 160–7.CrossRefGoogle Scholar
Cooper, E. S. & Bundy, D. A. P. (1988). Trichuris is not trivial. Parasitology Today 4, 301–6.CrossRefGoogle Scholar
Cooper, E. S., Whyte-Alleng, C. A. M., Finzi-Smith, J. S. & McDonald, T. T. (1992). Intestinal nematode infections in children: the pathophysiological price paid. Parasitology 104: S91–S103.CrossRefGoogle ScholarPubMed
Gamble, H. R., Purcell, J. P. & Fetterer, R. H. (1989). Purification of a 44 kDa protease that mediates ecdysis of infective Haemonchus contortus larvae. Molecular and Biochemical Parasitology 39, 31–8.Google Scholar
Greig, S. & Ashall, F. (1990). Electrophoretic characterisation of Trypanosoma cruzi peptidases. Molecular and Biochemical Parasitology 39, 31–8.CrossRefGoogle ScholarPubMed
Hill, D. E., Gamble, H. R., Rhoads, M. L., Fetterer, R. H. & Urban, J. F. (1993). Trichuris suis: a zinc metalloprotease from culture fluids of adult parasites. Experimental Parasitology 77, 170–8.CrossRefGoogle ScholarPubMed
Jenkins, S. N. & Wakelin, D. (1983). Functional antigens of Trichuris muris released during in vitro maintenance: their immunogenicity and partial purification. Parasitology 86, 73–8.CrossRefGoogle ScholarPubMed
Kusel, J. P. (1970). Studies on the structure and hatching of the eggs of Schistosoma mansoni. Parasitology 60, 79–88.CrossRefGoogle ScholarPubMed
Lacks, S. A. & Springhorn, S. S. (1980). Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Journal of Biological Chemistry 255, 7467–73.CrossRefGoogle Scholar
Lee, T. D. G. & Wakelin, D. (1982). Cortisone-induced immunotolerance to nematode infection in CBA/Ca mice. 1. Investigation into the defect in the protective response. Immunology 47, 227–32.Google Scholar
Lewert, R. M. & Lee, C. L. (1954). Studies on the passage of helminth larvae through host tissues. I. Histochemical studies on the extracellular changes caused by penetrating larvae. II. Enzymatic activity of larvae in vivo and in vitro. Journal of Infectious Diseases 95, 13–26.CrossRefGoogle Scholar
Marikovsky, M., Fishelson, Z. & Arnon, R. (1988). Purification and characterisation of proteases secreted by transforming schistosomula of Schistosoma mansoni. Molecular and Biochemical Parasitology 30, 45–54.CrossRefGoogle ScholarPubMed
McKerrow, J. H., Jones, P., Sage, H. & Pino-Heiss, S. (1985). Proteinases of invasive larvae of the trematode parasite Schistosoma mansoni degrade connective tissue and basement membrane macromolecules. The Biochemical Journal 231, 47–51.CrossRefGoogle ScholarPubMed
McKerrow, J. H., Brindley, P., Brown, M., Gam, A. A., Staunton, C. & Neva, F. A. (1990). Strongyloides stercoralis: identification of a protease that facilitates penetration of skin by the infective larvae. Experimental Parasitology 70, 134–43.CrossRefGoogle ScholarPubMed
Nimmo-Smith, R. H. & Keeling, J. E. D. (1960). Some hydrolytic enzymes of the parasitic nematode Trichuris muris. Experimental Parasitology 10, 337–55.CrossRefGoogle Scholar
Nokes, C., Grantham-Mcgregor, S. M., Sawyer, A. W., Cooper, E. S., Robinson, B. A. & Bundy, D. A. P. (1992). Moderate to heavy infections of Trichuris trichiura affect cognitive function in Jamaican schoolchildren. Parasitology 104, 539–47.CrossRefGoogle Scholar
Panesar, T. S. (1981). The early phase of tissue invasion by Trichuris muris (Nematoda: Trichuroidea). Zeitschrift für Parasitenkunde 66, 163–6.CrossRefGoogle ScholarPubMed
Ramsey, F. C. (1962). Trichuris dysentery syndrome. West Indian Medical Journal 11, 235–9.Google ScholarPubMed
Silen, J. L. & Agard, D. A. (1989). The α-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature, London 341, 462–4.CrossRefGoogle Scholar
Silberstein, D. S. & Despommier, D. D. (1984). Antigens from Trichinella spiralis that induce a protective response in the mouse. Journal of Immunology 132, 898–904.CrossRefGoogle ScholarPubMed
Wakelin, D. (1967). Acquired immunity to Trichuris muris in the albino laboratory mouse. Parasitology 57, 515–24.CrossRefGoogle ScholarPubMed