Hostname: page-component-8448b6f56d-qsmjn Total loading time: 0 Render date: 2024-04-18T05:41:37.677Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein antigens of Plasmodium knowlesi clones of different variant antigen phenotype

Published online by Cambridge University Press:  06 April 2009

R. J. Howard ,
Vivien Kao  and
J. W. Barnwell
R. J. Howard
Affiliation:
The Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205.
Vivien Kao
Affiliation:
The Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205.
J. W. Barnwell
Affiliation:
The Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20205.
Get access Rights & Permissions [Opens in a new window]

Summary

Mature asexual stages of the malaria parasite Plasmodium knowlesi synthesize proteins of Mr 180 000–225 000 that are expressed on the outer membrane of infected erythrocytes and which vary antigenically such that different parasite clones are specifically agglutinated with homologous antibody. Other non-agglutinable clones have been prepared which fail to express variant antigen on infected cells. Two agglutinable clones of different variant antigen phenotypes and a non-agglutinable clone were examined to determine the proportion of total malarial proteins represented by variant antigens. Malarial proteins were labelled with various radioactive amino acids and the sodium dodecyl sulphate—polyacrylamide gel patterns for the three clones compared by fluorography. The patterns were indistinguishable, the variant antigens being undetectable in analyses of total malarial proteins. Furthermore, these antigens were not detected by Coomassie Blue-staining of total cellular proteins after electrophoresis. Sodium dodecyl sulphate and Triton X-100 extracts of labelled cells were immunoprecipitated using a panel of sera of defined agglutination specificity. The variant antigens could not be detected in the fluorographic patterns of total malarial antigens immuno-precipitated by these sera. In contrast, after lactoperoxidase catalysed radio-iodination of intact schizont-infected cells, the 125 I-variant antigens on the cell surface were identified by demonstrating their accessibility both to antibody and to trypsin with intact cells. Thus, the variant antigens are quantitatively very minor malarial proteins that can only be detected by methods which selectively analyse the subset of proteins on the erythrocyte surface.

Type
Research Article
Information
Parasitology , Volume 88 , Issue 2 , April 1984 , pp. 221 - 237
Copyright
Copyright © Cambridge University Press 1984

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

Barnwell, J. W., Howard, R. J., Coons, H. G. & Miller, L. H. (1983). Splenic requirement for antigenic variation and expression of the variant antigen on the erythrocyte membrance in cloned Plasmodium knowlesi malaria. Infection and Immunity 40, 985–94.Google Scholar
Barnwell, J. W., Howard, R. J. & Miller, L. H. (1982 a). The influence of the spleen on the expression of surface antigens on parasitized erythrocytes. In Malaria and the Red Cell. Ciba Fdn Symp. 94, pp. 117–36. London.Google Scholar
Barnwell, J. W., Howard, R. J. & Miller, L. H. (1982 b). Altered expression of Plasmodium knowlesi variant antigen on the erythrocyte membrane in splenectomized rhesus monkeys. Journal of Immunology 128, 224–6.CrossRefGoogle ScholarPubMed
Brown, I. N., Brown, K. N. & Hills, L. A. (1968). Immunity to malaria: the antibody response to antigenic variation by Plasmodium knowlesi. Immunology 4, 127–38.Google Scholar
Brown, K. N. & Brown, I. N. (1965). Immunity to malaria: antigenic variation in chronic infections of Plasmodium knowlesi. Nature, London 208, 1286–8.CrossRefGoogle ScholarPubMed
Butcher, G. A. & Cohen, S. (1972). Antigenic variation and protective immunity in Plasmodium knowlesi malaria. Immunology 23, 503–21.Google ScholarPubMed
Chin, W., Contacos, P. G., Coatney, G. R. & Kimball, H. R. (1965). A naturally acquired quotidian-type malaria in man transferable to monkey. Science 149, 865.CrossRefGoogle Scholar
Cross, G. A. M. (1975). Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. Parasitology 71, 393–417.CrossRefGoogle ScholarPubMed
Dodge, J. T., Mitchell, C. & Hanahan, D. J. (1963). The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Archives of Biochemistry and Biophysics 100, 119–30.CrossRefGoogle ScholarPubMed
Eaton, M. C. (1938). The agglutination of Plasmodium knowlesi by immune serum. Journal of Experimental Medicine 67, 857–69.CrossRefGoogle ScholarPubMed
Epstein, N., Miller, L. H., Kaushal, D. C., Udeinya, I. J., Rener, J. R., Howard, R. J., Asofsky, R., Aikawa, M. & Hess, R. L. (1981). Monoclonal antibodies against a specific surface determinant on malarial (Plasmodium knowlesi) merozoites block erythrocyte invasion. Journal of Immunology 127, 212–17.CrossRefGoogle ScholarPubMed
Grant, P. T. & Fulton, J. D. (1957). The catabolism of glucose by strains of Trypanosoma rhodesiense. The Biochemical Journal 66, 242–50.Google Scholar
Hommel, M. & David, P. H. (1982). Plasmodium knowlesi variant antigens are found on schizont-infected erythrocytes but not on merozoites. Infection and Immunity 33, 275–84.CrossRefGoogle Scholar
Howard, R. J. & Barnwell, J. W. (1983). Solubilization and immunoprecipitation of 125I-antigens from Plasmodium knowlesi schizont-infected erythrocytes using nonionic, anionic and zwitterionic detergents. Parasitology 83, 27–36.Google Scholar
Howard, R. J., Barnwell, J. W., Kao, V., Daniel, W. A. & Aley, S. B. (1982 a). Radio-iodination of new protein antigens on the surface of Parasitology knowlesi schizont-infected erythrocytes. Molecular and Biochemical Parasitology 6, 343–67.CrossRefGoogle Scholar
Howard, R. J., Barnwell, J. W. & Kao, V. (1982 b). Tritiation of protein antigens of Plasmodium knowlesi schizont-infected erythrocytes using pyridoxal phosphate-sodium boro[3H]hydride. Molecular and Biochemical Parasitology 6, 369–87.Google Scholar
Howard, R. J., Barnwell, J. W. & Kao, V. (1983). Antigenic variation in Plasmodium knowlesi malaria: identification of the variant antigen on infected on infected erythrocytes. Proceedings of the National Academy of Sciences, USA 80, 4129–33.Google Scholar
Howard, R. J. & Kao, V. (1981). Comparison of the surface membrane proteins of human and rhesus monkey (Macaca mulatta) erythrocytes labelled with protein and glycoprotein radio-labelling probes. Comparative Biochemistry and Physiology 70B, 767–74.Google Scholar
Howard, R. J., Kaushal, D. C. & Carter, R. (1982). Radio-iodination of parasite antigens with 1, 3, 4, 6-tetrachloro-3α,6α-diphenylglycoluril (IODOGEN): studies with zygotes of Plasmodium gallinaceum. Journal of Protozoology 29, 114–17.CrossRefGoogle Scholar
Howard, R. J., Smith, P. M. & Mitchell, G. F. (1979). Identification of several differences between external proteins and glycoproteins of normal mouse (BALB/c) and human erythrocytes. Journal of Membrane Biology 49, 171–98.Google Scholar
Laemmli, U. K. & Favre, M. (1973). Maturation of the head of the head of bacteriophage T4. I. DNA packaging events. Journal of Molecular Biology 80, 575–99.Google Scholar
Langreth, S. A., Reese, R. T., Motyl, M. R. & Trager, W. (1979). Plasmodium falciparum: loss of knobs on the infected erythrocyte surface after long-term cultivation. Experimental Parasitology 48, 213–19.CrossRefGoogle ScholarPubMed
Vincent, H. M. & Wilson, R. J. M. (1980). Malarial antigens on infected erythrocytes. Transactions of the Royal Society of Tropical Medicine and Hygiene 74, 452–5.Google Scholar