Hostname: page-component-586b7cd67f-r5fsc Total loading time: 0 Render date: 2024-11-23T15:53:30.618Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein composition and protein synthesis in the surface membranes of Schistosoma mansoni

Published online by Cambridge University Press:  06 April 2009

J. R. Kusel
J. R. Kusel
Affiliation:
Division of Parasitology, National Institute for Medical Research, Mill Hill, London NW7 1AA
Get access Rights & Permissions [Opens in a new window]

Extract

Saponin treatment of cercariae and schistosomula alters the surface membrane so that it may be sheared from the organism and isolated as fragments by centrifugation. Saponin-calcium chloride treatment or freezing and thawing of adult worms removes the surface membrane, which can be washed from the bodies and collected by centrifugation. The small quantities of material available necessitated the development of a sensitive technique for detecting the proteins in the membranes. The surface membranes were radioiodinated after butan-1-ol extraction and electrophoresed in polyacrylamide gel. Adult surfaces prepared by the saponin-calcium chloride and by the freezing and thawing technique had identical protein components, detected as gel-cut profiles or in autoradiographs. The quantity of a rapidly migrating PAS-positive amido black negative component was greater in the surfaces prepared by saponincalcium chloride than in the frozen and thawed surfaces. This component contains lipid, some of which may be glycolipid. It was largely absent from the surface membranes of cercariae and schistosomula. Cercarial surface membranes contained a major protein component which was absent from the surface membranes of schistosomula. Otherwise the surface membranes of the cercariae were identical to those of the schistosomula in their protein components. The rate of incorporation of freshly synthesized protein per unit area of surface membrane of schistosomula was very low in the first 5 days in culture, after which there was a very rapid increase to a maximum rate on the 15th day. After this time, the rate of protein synthesis decreased to a low level at 26 days. In these studies the activity per unit area was measured and this would not be expected to vary greatly during growth. The biological significance of the observed variation in protein incorporation into the membrane is unclear.

Type
Research Article
Information
Parasitology , Volume 65 , Issue 1 , August 1972 , pp. 55 - 69
Copyright
Copyright © Cambridge University Press 1972

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Clegg, J. A., & Smithers, S. R., (1972). The effect of immune rhesus monkey serum on schistosomula of Schistosoma mansoni during cultivation in vitro. International Journal for Parasitology 2, 79–98.CrossRefGoogle ScholarPubMed
Clegg, J. A., Smithers, S. R., & Terry, R. J., (1971). Concomitant immunity and host antigens associated with schistosomes. International Journal for Parasitology 1, 43–9.CrossRefGoogle Scholar
Hochster, R. M. & Quastel, J. H. (eds.) (1963). Metabolic inhibitors, vol. 2. New York and London: Academic Press.Google Scholar
Hockley, D. J., & Mclaren, D. J., (1971). The outer membrane of Schistosoma mansoni. Transactions of the Royal Society of Tropical Medicine and Hygiene 65, 432.CrossRefGoogle ScholarPubMed
Hunter, W. M., & Greenwood, F. C., (1962). Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature 194, 495–6.CrossRefGoogle ScholarPubMed
Kusel, J. R., (1970). Studies on the surfaces of cercariae and schistosomula of Schistosoma mansoni. Parasitology 61, 127–34.CrossRefGoogle ScholarPubMed
Lenard, J., (1970). Protein and glycolipid components of human erythrocyte membranes. Biochemistry 9, 1129–32.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J., (1951). Protein-measurement with the folin phenol reagent. Journal of Biological Chemistry 193, 265–75.CrossRefGoogle ScholarPubMed
Maddy, A. H., (1964). The solubilization of the protein of the ox-erythrocyte. Biochimica et biophysica Acta 88, 448–9.Google ScholarPubMed
Marinetti, G. V., (1967). Lipid Chromatographic Analysis, vol. 1. London: Edward Arnold Ltd.Google Scholar
Morris, G. P., & Threadgold, L. T., (1968). Ultrastructure of the tegument of adult Schistosoma mansoni. Journal of Parasitology 54, 15–27.CrossRefGoogle ScholarPubMed
Schram, E., (1963). Organic Scintillation Detectors. Amsterdam, London, New York: Elsevier Publishing Co.Google Scholar
Shapiro, A. L., Vinuela, E., & Maizel, I. V., (1967). Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochemical and Biophysical Research Communications 28, 815–20.CrossRefGoogle ScholarPubMed
Smithers, S. R., & Terry, R. J., (1965). Infection of laboratory hosts with cercariae of Schistosoma mansoni and the recovery of adult worms. Parasitology 55, 695–700.CrossRefGoogle ScholarPubMed
Smithers, S. R., Terry, R. J., & Hockley, D. J., (1969). Host antigens in schistosomiasis. Proceedings of the Royal Society B 171, 483–94.Google ScholarPubMed
Stirewalt, M. A., (1963). Cercaria vs. schistosomule (Schistosoma mansoni). Absence of the pericercarial envelope in vivo and the early physiological and histological metamorphosis of the parasite. Experimental Parasitology 13, 395–406.CrossRefGoogle ScholarPubMed
Williams, J. G., & Gratzer, W. B., (1971). Limitations of detergent-polyaerylamide gel electrophoresis method for molecular weight determinations of proteins. Journal of Chromatography 57, 121–5.CrossRefGoogle ScholarPubMed
Work, T. S. & Work, E. (eds) (1969). Laboratory Techniques in Biochemistry and Molecular Biology, vol. 1. North-Holland Publishing Co.Google Scholar
Yang, S., & Criddle, R. S., (1970). In vitro biosynthesis of membrane proteins in isolated mitochondria from Saccharomyces carlsbergensis. Biochemistry 9, 3063–3072.CrossRefGoogle ScholarPubMed