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Physical and serological investigation of Rift Valley fever antigens

Published online by Cambridge University Press:  15 May 2009

Julia Levitt  and
A. Polson
Julia Levitt
Affiliation:
C.S.I.R. and U.C.T. Virus Research Unit, Medical School, Cape Town, South Africa
A. Polson
Affiliation:
C.S.I.R. and U.C.T. Virus Research Unit, Medical School, Cape Town, South Africa
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1. Extracts containing non-infective soluble antigens have been prepared from the tissues of mice infected with a pantropic or any of three neurotropic strains of Rift Valley fever virus. The antigens were detectable by complement-fixation and gel-precipitin tests using antisera prepared in mice.

2. The extracts appeared to contain at least two antigens separable by electrophoresis and distinguishable by Ouchterlony tests. The faster migrating minor antigen occurs sparsely and was not further examined.

3. No distinction, physical or immunological, was observed between the major antigen derived from the four strains.

4. In gel diffusion-filtration experiments with granulated 7 % agarose, the major antigen appeared to be polydisperse containing particles with diffusion rates ranging from at least as low as that of Burnupena cincta haemocyanin to almost as high as that of haemoglobin.

5. Centrifugal analysis indicated the presence of particles having sedimentation constants of about 8, 29 and greater than 100 Svedberg units. These particles have a density of about 1·27 g./ml. If all the particles of the major antigen are spherical, with a density of 1·27 g./ml., the three size groups have diameters of about 7–8, 14 and < 26 mμ.

6. The diffusion coefficient of the smallest particle was estimated to be 6·06x 10−7 cm.2/sec. corresponding to a sphere 7 mμ in diameter, or 4·78 x 10−7 cm.2/ corresponding to a sphere 9 mμ in diameter depending on which of two values for the diffusion coefficient of mouse γ-globulin is used in the calculation.

7. In density gradient zone electrophoresis at pH 8·6, the principal antigen migrated at about the same rate as haemoglobin and appreciably slower than the virus. The authors are indebted to Prof. A. Kipps for his continued interest in this work, and to Dr T. H. Mead for valuable criticism of this paper. This investigation was supported in part by a Public Health Service research grant Al 04044–02 from the National Institute of Health, Bethesda, U.S.A.

Type
Research Article
Information
Journal of Hygiene , Volume 62 , Issue 2 , June 1964 , pp. 239 - 256
Copyright
Copyright © Cambridge University Press 1964

References

REFERENCES

Allison, A. C. & Humphrey, J. H. (1959). Estimation of the size of antigens by gel diffusion methods. Nature, Lond., 183, 1590.CrossRefGoogle ScholarPubMed
Allison, A. C. & Humphrey, J. H. (1960). A theoretical and experimental analysis of double diffusion precipitation reactions in agar and its application to characterization of antigens. Immunology, 3, 95.Google Scholar
Andrews, P. (1962). Estimation of molecular weights of proteins by gel filtration. Nature, Lond., 196, 36.CrossRefGoogle ScholarPubMed
Casals, J. & Olitsky, P. K. (1950). A complement-fixation test for poliomyelitis virus. Proc. Soc. exp. Biol., N.Y., 75, 315.CrossRefGoogle ScholarPubMed
Casals, J., Olitsky, P. K. & Anslow, R. O. (1951). A specific complement-fixation test for infection with poliomyelitis virus. J. exp. Med. 94, 123.CrossRefGoogle ScholarPubMed
Clarke, D. H. & Casals, J. (1958). Techniques for hemagglutination and hemagglutination inhibition with arthropod-borne viruses. Amer. J. trop. Med. Hyg. 7, 561.CrossRefGoogle ScholarPubMed
Grabar, P. (1957). Agar-gel diffusion and immunoelectrophoretic analysis. Ann. N.Y. Acad. Sci. 69, 591.CrossRefGoogle ScholarPubMed
Kipps, A., Naudé, W. du T., Polson, A., Selzer, G. & van den Ende, M. (1957). The size distribution of specific antigens in virus-infected tissues and their significance. Ciba Foundation symposium on the nature of viruses, p. 224. Ed. Wolstenholme, G. E. W. and Millar, E. C. P.. London: J. and A. Churchill Ltd.Google Scholar
Largier, J. F. (1959). A purification and investigation of tetanus antitoxin. Arch. Biochem. Biophys. 77, 350.CrossRefGoogle Scholar
Levitt, J., Naudé, W. du T. & Polson, A. (1963). Purification and electron microscopy of pantropic Rift Valley fever virus. Virology, 20, 530.CrossRefGoogle ScholarPubMed
Mansi, W. (1957). The study of some viruses by the plate gel diffusion precipitin test. J. comp. Path. 67, 297.CrossRefGoogle Scholar
Mayer, M. M., Osler, A. G., Bier, O. G. & Heidelberger, M. (1946). The activating effect of magnesium and other cations on the hemolytic function of complement. J. exp. Med. 84, 535.CrossRefGoogle ScholarPubMed
Mead, T. H. (1962). Purification of rabies soluble antigen. J. gen. Microbiol. 27, 397.CrossRefGoogle Scholar
Ouchterlony, C. F. (1953). Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta path. microbiol. scand. 32, 231.CrossRefGoogle ScholarPubMed
Pereira, M. S., Pereira, H. G. & Allison, A. C. (1959). Use of gel diffusion precipitation test in the diagnosis of adenovirus infections. Lancet, i, 551.CrossRefGoogle Scholar
Polson, A. (1958). A method for determination of diffusion coefficients by the gel precipitin technique. Biochim. biophys. Acta, 29, 426.CrossRefGoogle ScholarPubMed
Polson, A. (1961 a). Fractionation of protein mixtures on columns of granulated agar. Biochim. biophys. Acta, 50, 565.CrossRefGoogle ScholarPubMed
Polson, A. (1961 b). A simplified fraction collector for gradient elution chromatography. J. Chromatog. 5, 116.CrossRefGoogle Scholar
Polson, A. & Cramer, R. (1958). Zone electrophoresis of type 1 poliomyelitis virus. Biochim. biophys. Acta, 29, 188.CrossRefGoogle Scholar
Polson, A. & Deeks, D. (1960). The diffusion constants of rabbit, guinea-pig and rat antibodies to a single common antigen. Biochim. biophys. Acta, 39, 208.CrossRefGoogle ScholarPubMed
Polson, A. & Deeks, D. (1962). Zone electrophoresisofentero-viruses. J. Hyg., Camb., 60,217.CrossRefGoogle Scholar
Polson, A. & Hamton, J. W. F. (1960). Determination of the diffusion constant of poliovirus by the gel precipitin technique. Biochim. biophys. Acta, 44, 18.CrossRefGoogle ScholarPubMed
Polson, A. & Levitt, J. (1963 a). Density determination in a preformed gradient of caesium chloride. Biochim. biophys. Acta, 75, 88.CrossRefGoogle Scholar
Polson, A. & Levitt, J. (1963 b). A slowly sedimenting infectious component of Rift Valley fever virus. J. Hyg., Camb., 61, 451.Google ScholarPubMed
Polson, A. & Linder, A. M. (1953). The determination of sedimentation constants of proteins and viruses with the help of the Spinco preparative ultracentrifuge. Biochim. biophys. Acta, 11, 199.CrossRefGoogle ScholarPubMed
Polson, A. & Madsen, T. (1954). Particle size distribution of African horsesickness virus. Biochim. biophys. Acta, 14, 366.CrossRefGoogle ScholarPubMed
Polson, A. & Madsen, T. (1955). A brain factor influencing the viability of neurotropic Rift Valley fever. Nature, Lond., 176, 645.CrossRefGoogle ScholarPubMed
Polson, A. & Potgieter, G. M. (1964). Determination of diffusion constants by a multiunit analytical method. Nature, Lond. (in the Press).CrossRefGoogle ScholarPubMed
Polson, A., Selzer, G. & van den Ende, M. (1957). The electrophoretic mobilities of adapted MEF1 poliomyelitis virus and its soluble antigen. Biochim. biophys. Acta, 24, 600.CrossRefGoogle ScholarPubMed
Russell, B., Mead, T. H. & Polson, A. (1964). A method of preparing agarose. Biochim. biophys. Acta (in the Press).CrossRefGoogle ScholarPubMed
Smithburn, K. C. (1949). Rift Valley fever. Neurotropic adaptation of the virus and the experimental use of the modified virus as a vaccine. Brit. J. exp. Path. 30, 1.Google ScholarPubMed
Steere, R. L. & Ackers, G. K. (1962). Restricted-diffusion chromatography through calibrated columns of granulated agar gel; a simple method for particle size determination. Nature, Lond., 196, 475.CrossRefGoogle Scholar
van Regenmortel, M. H. V. (1959). Determination of diffusion coefficient of turnip yellow mosaic virus by the gel precipitin technique. Biochim. biophys. Acta, 34, 553.CrossRefGoogle ScholarPubMed
van Regenmortel, M. H. V. (1961). Zone electrophoresis and particle size of cucumber mosaic virus. Virology, 15, 221.CrossRefGoogle ScholarPubMed
Wilson, M. W. & Pringle, B. H. (1954). Experimental studies of the agar-plate precipitin test of Ouchterlony. J. Immunol. 73, 232.CrossRefGoogle ScholarPubMed