Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-15T01:48:29.405Z Has data issue: false hasContentIssue false

A quantitative comparison of the sensitivity of serological tests for bovine brucellosis to different antibody classes

Published online by Cambridge University Press:  15 May 2009

G. S. Allan
Affiliation:
'Attwood' Veterinary Research Laboratory, Victorian Department of Agriculture Westmeadows, Victoria 3047, Australia
R. J. Chappel
Affiliation:
'Attwood' Veterinary Research Laboratory, Victorian Department of Agriculture Westmeadows, Victoria 3047, Australia
P. Williamson
Affiliation:
'Attwood' Veterinary Research Laboratory, Victorian Department of Agriculture Westmeadows, Victoria 3047, Australia
D. J. McNaught
Affiliation:
'Attwood' Veterinary Research Laboratory, Victorian Department of Agriculture Westmeadows, Victoria 3047, Australia
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Brucella-specific antibodies of different immunoglobulin classes were quantitatively evaluated with respect to their efficiency in serological tests for bovine brucellosis.

IgM reacted more efficiently than IgG1 and IgG2 in both the Rose Bengal plate test and serum agglutination test. The complement fixation test was found to be slightly more sensitive to IgM than to IgG1 and did not react to IgG2. IgM was, however, partly inactivated when heated at 60°C. in the presence of serum.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1976

References

REFERENCES

Alton, G. G. & Jones, L. M. (1967). Laboratory techniques in brucellosis. World Health Organization Monograph Series no. 55, Geneva.Google Scholar
Alton, G. G., Maw, J., Rogerson, B. A. & McPherson, G. G. (1975). The serological diagnosis of bovine brucellosis: an evaluation of the complement fixation, serum agglutination and Rose Bengal tests. Australian Veterinary Journal 51, 57.CrossRefGoogle ScholarPubMed
Beh, K. J. (1974). Quantitative distribution of Brucella antibody amongst immunoglobulin classes in vaccinated and infected cattle. Research in Veterinary Science 17, 1.CrossRefGoogle ScholarPubMed
Cho, H. J. & Ingram, D. G. (1972). Mechanisms of prozone formation in agglutination reaction. Canadian Journal of Microbiology 18, 449.CrossRefGoogle ScholarPubMed
Corbel, M. J. (1972 a). Characterisation of antibodies active in the Rose Bengal plate test. Veterinary Record 90, 484.CrossRefGoogle ScholarPubMed
Corbel, M. J. (1972 b). Identification of the immunoglobulin class active in the Rose Bengal plate test for bovine brucellosis. Journal of Hygiene 70, 779.Google ScholarPubMed
Corbel, M. J. (1973). Studies on the mechanism of the Rose Bengal plate test for bovine brucellosis. British Veterinary Journal 129, 157.CrossRefGoogle ScholarPubMed
Curtain, C. C. (1971). The influence of environment upon serum immunoglobulin levels in cattle. British Veterinary Journal 127, 442.CrossRefGoogle ScholarPubMed
Davies, G. (1971). The Rose Bengal test. Veterinary Record 88, 447.CrossRefGoogle ScholarPubMed
Davis, B. J. (1964). Disc electrophoresis. II. Method and application to human serum proteins. Annals of the New York Academy of Sciences 121, 404.CrossRefGoogle ScholarPubMed
Elberg, S. S. (1973). Immunity to Brucella infection. Medicine, Baltimore 52, 339.CrossRefGoogle ScholarPubMed
Hess, W. R. (1953 a). Studies on a non-specific Brucella-agglutinating substance in bovine serum. I. The differentiation of the specific and non-specific agglutinins by heat treatment. American Journal of Veterinary Research 14, 192.Google Scholar
Hess, W. R. (1953 b). Studies on a non-specific Brucella-agglutinating substance in bovine serum. II. Isolation and purification of the Brucella-agglutinating substances. American Journal of Veterinary Research 14, 195.Google Scholar
Kulshreshtha, R. C., Atal, P. R. & Wahi, P. N. (1973). A study on serological tests for the diagnosis of human and bovine brucellosis. Indian Journal of Medical Research 61, 1471.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265.CrossRefGoogle ScholarPubMed
Marchalonis, J. J. (1969). An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochemical Journal 113, 299.CrossRefGoogle ScholarPubMed
Miller, J. K., Nettleton, P. F. & Robertson, A. M. (1973). Evaluation of a two-channel automated system for the sero-diagnosis of brucellosis. Veterinary Record 92, 492.CrossRefGoogle ScholarPubMed
Morgan, W. J. (1969). Brucellosis in animals: diagnosis and control. Proceedings of the Royal Society of Medicine 62, 1050.CrossRefGoogle ScholarPubMed
Rice, C. E. & Boyes, B. (1971). Serum immunoglobulins in bovine brucellosis. New Zealand Veterinary Journal 19, 146.Google ScholarPubMed
Rose, J. E. & Roepke, M. H. (1957). An acidified antigen for detection of non-specific reactions in the plate-agglutination test for bovine brucellosis. American Journal of Veterinary Research 18, 550.Google Scholar