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Characterization of surface proteins and glycoproteins on red blood cells from mice infected with haemosporidia: Plasmodium yoelii infections of BALB/c mice

Published online by Cambridge University Press:  06 April 2009

R. J. Howard ,
Patricia M. Smith  and
G. F. Mitchell
R. J. Howard
Affiliation:
The Laboratory of Immunoparasitology, The Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital P.O., Victoria 3050, Australia
Patricia M. Smith
Affiliation:
The Laboratory of Immunoparasitology, The Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital P.O., Victoria 3050, Australia
G. F. Mitchell
Affiliation:
The Laboratory of Immunoparasitology, The Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital P.O., Victoria 3050, Australia
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Summary

Lactoperoxidase-catalysed radio-iodination was used to compare the surface proteins on red cells from Plasmodium yoelii-infected and normal BALB/c mice. The profile of radio-iodinated proteins separated by SDS-polyacrylamide gel electrophoresis was different for infected blood of similar parasitaemia from mice inoculated with different doses of the parasite. Inoculation with the lower dose resulted in the appearance of a major radio-iodinated protein of apparent molecular weight (Mr) 76000 which was labelled to a similar extent on uninfected red cells from infected blood and purified multinucleate infected cells. Several minor radio-iodinated bands, with identical mobilities to the minor bands on normal BALB/c erythrocytes, were also present on red cells from this infected blood. In contrast, the higher inoculation dose produced changes in the minor labelled bands, and the band with Mr of 76000 was absent. In this case, the minor radio-iodinated proteins of the normal BALB/c erythrocyte (with Mr of 65000, 57000, 48000, 38000 and 32000) were replaced by a series of bands with Mr of 60000, 50000, 43000 and 28000 on both uninfected and infected red cells. These differences with inoculation dose may be related to the different duration of these infections, the development of anaemia and the extent of pathological changes at the erythrocyte surface. P. yoelii infection caused a marked loss in periodate-dependent labelling of sialoglycoproteins on most, if not all, red cells in infected blood. There was also a large decrease in galactose oxidase-dependent glycoprotein labelling with or without neuraminidase treatment. These changes in the carbohydrate groups on red cell membrane glycoproteins may be linked to the excessive loss of both uninfected and infected red cells during some malaria infections.

Type
Research Article
Information
Parasitology , Volume 81 , Issue 2 , October 1980 , pp. 299 - 314
Copyright
Copyright © Cambridge University Press 1980

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References

REFERENCES

Barker, L. R. (1971). Acquired immunity to Plasmodium berghei yoelii in mice. Transactions of the Royal Society of Tropical Medicine and Hygiene 65, 586–90.CrossRefGoogle ScholarPubMed
Brown, K. N. & Hills, L. A. (1979). The possible role of isoantigens in protective immunity to malaria. WHO Conference Proceedings on the Immunology of Malaria (in the Press).Google ScholarPubMed
Brown, I. N., Brown, K. N. & Hills, L. A. (1968). Immunity to malaria; the antibody response to antigen variation by Plasmodium knowlesi. Immunology 14, 127–38.Google ScholarPubMed
Butcher, G. A. & Cohen, S. (1972). Antigen variation and protective immunity-in Plasmodium knowlesi malaria. Immunology 23, 503–21.Google ScholarPubMed
Clark, I. A. & Allison, A. C. (1974). Babesia microti and Plasmodium berghei yoelii infections in nude mice. Nature, London 252, 328–9.CrossRefGoogle ScholarPubMed
Cox, F. E. G. (1970). The specificity of immunoglobulin G and immunoglobulin M in the fluorescent-antibody test for malaria parasites in mice. Bulletin of the World Health Organization 43, 341–4.Google ScholarPubMed
Fairbanks, G., Steck, T. L. & Wallach, D. F. H. (1971). Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10, 2606–17.CrossRefGoogle ScholarPubMed
Freeman, R. R. & Parish, C. R. (1978). Spleen cell changes during fatal and self-limiting malarial infections of mice. Immunology 35, 479–84.Google ScholarPubMed
Gahmberg, C. G. (1976). External labelling of human erythrocyte glycoproteins. Studies with galactose oxidase and fluorography. Journal of Biological Chemistry 251, 510–15.CrossRefGoogle ScholarPubMed
Gahmberg, C. G. & Hakomori, S. (1973). External labelling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes. Journal of Biological Chemistry 248, 4311–17.CrossRefGoogle ScholarPubMed
Glossman, H. & Neville, D. M. (1971). Glycoproteins of cell surfaces. Comparative study of three different cell surfaces of the rat. Journal of Biological Chemistry 246, 6339–46.Google Scholar
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1978). Removal of leucocytes from red cells in Plasmodium berghei-infected mouse blood and purification of schizont-infected cells. Annals of Tropical Medicine and Parasitology 72, 573–6.CrossRefGoogle ScholarPubMed
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1979 a). Identification of several differences between external proteins and glycoproteins of normal mouse (BALB/c) and human erythrocytes. Journal of Membrane Biology 49, 171–98.CrossRefGoogle ScholarPubMed
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1979 b). Optimal conditions for lactoperoxidase catalyzed radioiodination of external proteins on mouse erythrocytes. Australian Journal of Experimental Biology and Medical Science 57, 355–68.CrossRefGoogle ScholarPubMed
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1980 a). Characterization of surface proteins and glycoproteins on red blood cells from mice infected with haemosporidia: Babesia rodhaini infections of BALB/c mice. Parasitology 81, 251–71.CrossRefGoogle ScholarPubMed
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1980 b). Characterization of surface proteins and glycoproteins on red blood cells from mice infected with haemosporidia: Plasmodium berghei infections of BALB/c mice. Parasitology 81, 273–98.CrossRefGoogle ScholarPubMed
Jayawardena, A. N., Targett, G. A. T., Carter, R. L., Leuchars, E. & Davies, A. J. S. (1977). The immunological response of CBA mice to P. yoelii. I. General characteristics, the effects of T cell deprivation reconstruction with thymus grafts. Immunology 32, 849–59.Google Scholar
Jayawardena, A. N., Targett, G. A. T., Leuchars, E. & Davies, A. J. S. (1978). The immunological response to CBA mice to P. yoelii II. The passive transfer to immunity with serum and cells. Immunology 34, 157–65.Google Scholar
Jayawardena, A. N., Targett, G. A. T., Leuchars, E., Doenhoff, M. J., Carter, R. L. & Davies, A. J. S. (1975). T cell activation in murine malaria. Nature, London 258, 149–51.CrossRefGoogle ScholarPubMed
Konigk, E. & Mirtsch, S. (1977). Plasmodium chabaudi-infection of mice; specific activities of erythrocyte membrane-associated enzymes and patterns of proteins and glycoproteins of erythrocyte membrane preparations. Tropenmedizin und Parasitologie 28, 17–22.Google ScholarPubMed
Ladda, R., Aikawa, M. & Sprinz, H. (1969). Penetration of erythrocytes by merozoites of mammalian and avian malarial parasites. Journal of Parasitology 55, 633–44.CrossRefGoogle ScholarPubMed
Mitchell, G. F., Handman, E. & Howard, R. J. (1978). Protection of mice against plasmodium and babesia infections: attempts to raise host-protective sera. Australian Journal of Experimental Biology and Medical Science 56, 553–9.CrossRefGoogle ScholarPubMed
Nomoto, M., Narahashi, Y. & Murakami, M. (1960). A proteolytic enzyme of Streptomyces griseus. VI. Hydrolysis of protein by Streptomyces griseus protease. Journal of Biochemistry, Tokyo 48, 593–602.CrossRefGoogle Scholar
Playfair, J. H. L., DeSouza, J. B. & Cottrell, B. J. (1977). Reactivity and cross-reactivity of mouse helper T cells to malaria parasites. Immunology 32, 681–7.Google ScholarPubMed
Roberts, D. W., Rank, R. G., Weidanz, W. P. & Finnerty, J. F. (1977). Prevention of recrudescent malaria in nuce mice by thymic grafting or by treatment with hyperimmune serum. Infection and Immunity 16, 821–6.CrossRefGoogle ScholarPubMed
Schauer, R. & Faillard, J. (1968). Das verhalten isomerer N, O-Diacetyl-neruaminisauregly-koside in Submaxillarismucin von Pferd und Rind bei Einwirkung bakterieller Neuraminidase. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 349, 961–8.CrossRefGoogle ScholarPubMed
Schubert, D. (1970). Immunoglobulin biosynthesis. IV. Carbohydrate attachment to immunoglobulin subunits. Journal of Molecular Biology 51, 287–301.CrossRefGoogle ScholarPubMed
Trop, M. & Birk, Y. (1970). The specificity of proteinases from Streptomyces griseus (Pronase). The Biochemical Journal 116, 19–25.CrossRefGoogle ScholarPubMed
Wedderburn, N. (1974). Parasites in the Immunized Host: Mechanisms of Survival. Amsterdam: Associated Scientific Publishers.Google Scholar
Weidekamm, E., Wallach, D. F. H., Lin, P.-S. & Hendricks, J. (1973). Erythrocyte membrane alterations due to infection with Plasmodium berghei. Biochimica et biophysica acta 323, 539–46.CrossRefGoogle ScholarPubMed
Weinbaum, F. I., Evans, C. B. & Tigelaar, R. E. (1976 a). Immunity to Plasmodium berghei yoelii in mice. I. The course of infection in T cell and B cell deficient mice. Journal of Immunology 117, 1999–2005.CrossRefGoogle Scholar
Weinbaum, F. T., Evans, C. B. & Tigelaar, R. E. (1976 b). An in vitro assay for T cell immunity to malaria in mice. Journal of Immunology 116, 1280–3.CrossRefGoogle Scholar