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The immune response to viruses in calves: I. Response to Murray Valley encephalitis virus

Published online by Cambridge University Press:  15 May 2009

C. J. Sanderson
Affiliation:
Department of Preventive Medicine, University of Queensland, St Lucia, Queensland, Australia
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Following inoculation of Murray Valley encephalitis virus into calves there was an early transient IgM response. The appearance of IgG was only slightly later than the first appearance of IgM in three calves, and in one calf IgG was detected before IgM. The secondary response was characterized by the more rapid appearance of IgG and the virtual absence of IgM. The IgG was of the electrophoretically fast type; there was an almost insignificant amount of antibody activity in electrophoretically slow fractions. IgM and slow IgG had no complement-fixing activity. IgM and IgG showed different cross-reactions to other group B arboviruses. The different cross-reactions, and the appearance of IgG before IgM in one animal suggests that the switch-over from IgM to IgG synthesis in the response is not the result of either a total or a random proportion of cells producing IgM, changing to IgG production. The fact that the IgG was almost exclusively of fast electrophoretic mobility suggested that the virus antigenic components were strongly basic, and as this is contrary to the chromatographic properties of arboviruses, it is suggested that the virus particles must be broken down before making contact with the factors determining the type of immunoglobulin formed.

Type
Original Articles
Copyright
Copyright © Cambridge University Press 1968

References

Boulanger, P. & Bannister, G. L. (1960). A modified direct complement fixation test for the detection of antibodies in the serum of cattle previously infected with vesicular stomatitis virus. J. Immun. 85, 368.CrossRefGoogle Scholar
Britten, R. J. & Roberts, R. B. (1960). High resolution density gradient sedimentation analysis. Science, N.Y. 131, 32.CrossRefGoogle ScholarPubMed
Buescher, E. L., Scherer, W. F., Grossberg, S. E., Chanock, R. M. & Philpot, V. B. (1959). Immunologic studies of Japanese encephalitis virus in Japan. I. Antibody responses following overt infections in man. J. Immun. 83, 582.CrossRefGoogle Scholar
Clark, D. H. & Casals, J. (1958). Techniques for the haemagglutination and haemagglutination-inhibition tests with arthropod-borne viruses. Am. J. trop. Med. Hyg. 7, 561.CrossRefGoogle Scholar
Davenport, F. M. & Hennessy, A. V. (1956). A serologic recapitulation of past experiences with influenza A; antibody response to monovalent vaccine. J. exp. Med. 104, 85.CrossRefGoogle ScholarPubMed
Davis, B. J. (1964). Disk electrophoresis: Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121, 404.CrossRefGoogle ScholarPubMed
Dixon, F. J. & Maurer, P. H. (1955). Specificity of the secondary response to protein antigens. J. Immun. 74, 418.CrossRefGoogle ScholarPubMed
Finkelstein, M. S. & Uhr, J. W. (1964). Specific inhibition of antibody formation by passively administered 19S and 7S antibody. Science, N.Y. 146, 67.CrossRefGoogle Scholar
Gilden, R. V. & Tokuda, S. (1963). Antibody quality after sequential immunization with related antigens. Science, N. Y. 140, 405.CrossRefGoogle ScholarPubMed
Kunkel, H. G. (1960). In The Plasma Proteins, vol. I (ed. Putman, F. W.), p. 279. New York and London: Academic Press.CrossRefGoogle Scholar
Murphy, F. A., Osebold, J. W. & Aalund, O. (1965). Physical heterogeneity of bovine gamma-globulins: characterization of gamma-M and gamma-G globulins. Archs Biochem. Biophys. 112, 126.Google Scholar
Murphy, F. A., Osebold, J. W. & Aalund, O. (1966). Kinetics of the response to Anaplasma marginale infection. J. infect. Dis. 116, 99.Google Scholar
Nicoli, J. (1965). Chromatographie sur celluloses échangeuses d'ions et gel-filtration sur agarose d'arbovirus et de produits extraits de ces arbovirus. Annls Inst. Pasteur, Paris 108, 695.Google Scholar
Nossal, G. J. V., Austin, C. M. & Ada, G. L. (1965). Antigens in immunity. VII. Analysis of immunological memory. Immunology 9, 333.Google ScholarPubMed
Nossal, G. J. V., Szenberg, A., Ada, G. L. & Austin, C. M. (1964). Single cell studies on 19S antibody production. J. exp. Med. 119, 485.CrossRefGoogle ScholarPubMed
Pierce, A. E. & Feinstein, A. (1965). Biophysical and iirununological studies on bovine immune globulins with evidence for selective transport within the mammary gland from maternal plasma to colostrum. Immunology 8, 106.Google ScholarPubMed
Pond, W. L., Ehrenkranz, N. J., Danauskas, J. X. & Carter, M. J. (1967). Heterotypic serological responses after yellow fever vaccination; detection of persons with past St Louis encephalitis or dengue. J. Immun. 98, 673.Google Scholar
Porterfield, J. S. (1962). The nature of serological relationships among arthropod-borne viruses. Adv. Virus Res. 9, 127.CrossRefGoogle Scholar
Sanderson, C. J. (1968 a). The immune response to viruses in calves. II. The response in young calves. J. Hyg., Camb. 66, 461.CrossRefGoogle ScholarPubMed
Sanderson, C. J. (1968 b). Arbovirus non-specific inhibitors and natural agglutinins in bovine serum. Res. vet. Sci. 9, 400.CrossRefGoogle ScholarPubMed
Scherer, W. F., Kltaoka, M., Grossberg, S. E., Okuna, T., Ogata, T. & Chanock, R. M. (1959). Immunologic studies of Japanese encephalitis virus in Japan. II. Antibody response following inapparent human infection. J. Immun. 83, 594.CrossRefGoogle ScholarPubMed
Schoenberg, M. D., Stavitsky, A. B., Moore, H. D. & Freeman, M. J. (1965). Cellular sites of synthesis of rabbit immunoglobulins during primary response to diphtheria toxoid-Freunds adjuvant. J. exp. Med. 121, 577.CrossRefGoogle ScholarPubMed
Sela, M. & Mozes, E. (1966). Dependence of the chemical nature of antibodies on the net electrical charge of antigens. Proc. natn. Acad. Sci. U.S.A. 55, 445.CrossRefGoogle ScholarPubMed
Southam, C. M. & Green, E. L. (1958). Clinical application of the haemagglutination-inhibition test for West Nile virus antibodies. J. infect. Dis. 102, 174.Google Scholar
Svehag, S. E. & Mandel, B. (1964 a). The formation and properties of poliovirus-neutralizing antibody. I. 19S and 7S antibody formation: differences in kinetics and antigen dose requirement for induction. J. exp. Med. 119, 1.Google Scholar
Svehag, S. E. & Mandel, B. (1964 b). The formation and properties of poliovirus-neutralizing antibodies. II. 198 and 7S antibody formation: differences in antigen dose requirement for sustained synthesis, anamnesis and sensitivity to X-irradiation. J. exp. Med. 119, 21.Google Scholar
Theiler, M. & Cassals, J. (1958). The serological reactions in yellow fever. Am. J. trop. Med. Hyg. 7, 585.Google Scholar
Uhr, J. W. (1964). The heterogeneity of the immune response. Science, N.Y. 145, 457.CrossRefGoogle ScholarPubMed
Uhr, J. W. & Finkelstein, M. S. (1967). The kinetics of antibody formation. Prog. Allergy 10, 37.Google ScholarPubMed
Webster, R. G. (1966). Original antigenic sin in ferrets: the response to sequential infections with influenza viruses. J. Immun. 97, 177.CrossRefGoogle Scholar
Westaway, E. G. (1966). Assessment and application of a cell line from pig kidney for plaque assay and neutralization tests with twelve group B arboviruses. Am. J. Epidem. 84, 439.Google Scholar
Wiegle, W. O. (1961). Immunochemical properties of the cross-reactions between anti-BSA and heterologous albumins. J. Immun. 87, 599.Google Scholar
Winter, A. J. (1966). Characterization of the antibody for Vibrio fetus endotoxin in sera of normal and V. fetus infected cattle. J. Immun. 95, 1002.Google Scholar