Hostname: page-component-7c8c6479df-8mjnm Total loading time: 0 Render date: 2024-03-27T21:27:34.168Z Has data issue: false hasContentIssue false

Antibodies to the glutamate dehydrogenase of Plasmodium falciparum

Published online by Cambridge University Press:  06 April 2009

I. T. Ling
Affiliation:
National institute for Medical Research, Mill Hill, London
S. Cooksley
Affiliation:
Brunel University, Department of Applied Biology, Uxbridge, Middlesex
P. A. Bates
Affiliation:
National institute for Medical Research, Mill Hill, London
E. Hempelmann
Affiliation:
Institut für Biochemie II, Im Neuenheimer Feld 328 D-6900, Heidelberg 1, FRG
R. J. M. Wilson
Affiliation:
National institute for Medical Research, Mill Hill, London

Summary

Polyclonal antisera raised against Plasmodium knowlesi reacted with (1) NADP-specific glutamate dehydrogenase (GLDH) of P. knowlesi, (2) GLDH of P. falciparum and (3) GLDH of Proteus spp. The antisera did not react with NAD(P) GLDH from bovine liver. Polyclonal antisera raised against the GLDH of Proteus spp. cross-reacted with GLDH from P. falciparum. Monoclonal antibodies (McAbs) obtained from mice immunized with Proteus GLDH were either specific for the bacterial enzyme or cross-reacted with P. falciparum GLDH. The selected McAbs did not react with GLDI-1 from P. knowlesi, P. chabaudi or P. berghei. The GLDH of P. falciparum was shown to be a cytosolic protein (by FAT) with a subunit molecular weight of approximately 49000 Da (by immunoprecipitation) having a pre dominantly hexameric form (by sucrose density gradient). Implications of the conserved sequences of GLDHs and other enzymes are discussed.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1986

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

Brett, M., Chambers, G. K., Holder, A. A., Fincham, J. R. S. & Wooton, J. C. (1976). Mutational amino acid replacements in Neurospora crassa NADP-specific glutamate dehydrogenase. Journal of Molecular Biology 106, 122.CrossRefGoogle ScholarPubMed
Dluzewski, A. R., Ling, I. T., Rangachari, K., Bates, P. A. & Wilson, R. J. M. (1984). A simple method for isolating viable mature parasites of Plasmodium falciparum from cultures. Transactions of the Royal Society of Tropical Medicine and Hygiene 78, 622–4.CrossRefGoogle ScholarPubMed
Elford, B. C., Hayes, J. D., Chulay, J. D. & Wilson, R. J. M. (1985). Stage-specific transport and metabolism of L-glutamine induced by Plasnzodium falciparum in human red cells. Molecular and Biochemical Parasitology (in the Press).Google Scholar
Fahien, L. A., Steinman, H. G. & McCann, R. (1966). Immunochemical studies of bovine and frog liver glutamate dehydrogenases. Journal of Biological Chemistry 241, 4700–9.CrossRefGoogle ScholarPubMed
Galfre, G., Howe, J. C., Milstein, C., Butcher, G. W. & Howard, J. C. (1977). Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature, London 266, 550–2.CrossRefGoogle ScholarPubMed
Hempelmann, E., Ling, I. & Wilson, R. J. M. (1981). S-antigens and isozymes in strains of Plasmodium falciparum. Transactions of the Royal Society of Tropical Medicine and Hygiene 75, 855–8.CrossRefGoogle ScholarPubMed
Hempelmann, E., Putfarken, B., Rangachari, K. & Wilson, R. J. M. (1986). Immunoprecipitation of malarial acid endopeptidase. Parasitology 92, 305–12.CrossRefGoogle ScholarPubMed
Hempelmann, E. & Wilson, R. J. M. (1980). Endopeptidases from Plasmodium knowlesi. Parasitology 80, 323–30.CrossRefGoogle ScholarPubMed
Hempelmann, E. & Wilson, R. J. M. (1982). Immunoprecipitation of malarial enzymes. Journal of Protozoology 29, 637.Google Scholar
Horejsi, V. & Hilgent, I. (1983). Nitrocellulose membrane as an antigen or antibody carrier for screening hybridoma cultures. Journal of Immunological Methods 62, 325–9.CrossRefGoogle ScholarPubMed
Kemp, D. J., Corcoran, I. M., Coppel, R. L., Stahl, H. D., Bianco, A. E., Brown, C. V. & Anders, R. F. (1985). Size variation in chromosomes from independent cultured isolates of Plasmodium falciparum. Nature, London 315, 347–9.CrossRefGoogle ScholarPubMed
Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, London 227, 680–5.CrossRefGoogle ScholarPubMed
Martinez-Ramon, A. & Renau-Piqueras, J. (1984). Monoclonal antibody to glutamate dehydro genase. Isolation and characterisation. Cell Biology International Reports 8, 665–74.CrossRefGoogle Scholar
Mattaj, I. W., McPherson, M. J. & Wootton, J. C. (1982). Localisation of a strongly conserved section of coding sequence in glutamate dehydrogenase genes. Federation of European Biochemical Societies, Letters 147, 21–5.CrossRefGoogle ScholarPubMed
McCutchan, T. F., Dame, J. B., Miller, L. H. & Barnwell, J. (1984). Evolutionary relatedness of Plasmodium species as determined by the structure of DNA. Science 225, 808–11.CrossRefGoogle ScholarPubMed
Roberts, D. B. & Pateman, J. A. (1964). Immunological studies of amination deficient strains of Neurospora crassa. Journal of General Microbiology 34, 295305.CrossRefGoogle Scholar
Schmidt, E. (1974). Glutamate dehydrogenase U.V.-assay. In Methods of Enzymatic Analysis, vol. 2, (ed. Bergmeyer, H. U.), pp. 650–6. New York: Academic Press.CrossRefGoogle Scholar
Sherman, I. W. (1979). Biochemistry of Plasmodium (malarial parasites). Microbiological Reviews 43, 453–95.CrossRefGoogle ScholarPubMed
Smith, E. L., Austen, B. M., Blumsntithal, K. M. & Nyc, J. F. (1975). Glutamate dehydrogenases. In The Enzymes, vol. 11 (ed. Boyer, P. D.), pp. 293367. New York: Academic Press.Google Scholar
Walliker, D. (1983). The Contribution of Genetics of the Study of Parasitic Protozoa. London: Research Studies Press Ltd. John Wiley.Google Scholar
Walter, R. D., Nordmeyer, J.-P. & Königk, E. (1974). NADP-specific glutamate dehydrogenase from Plasmodium chabaudi. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 355, 495500.Google ScholarPubMed