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Detection of Antibodies to the Basic Protein of Human Myelin by Radioimmunoassay and Immunofluorescence^1,2,

Clinical Research Unit, The Walter and Eliza Hall Institute of Medical Research, and the Russell Grimwade School of Biochemistry, University of Melbourne, Victoria, Australia

Abstract

Specific antibodies to a basic protein that is a component of myelin were demonstrated quantitatively by gel filtration radioimmunoassay in three species, rabbit, guinea pig and rat, after a single immunization with the antigen in complete Freund's adjuvant. In the rabbit, the antibody to ¹²⁵I-labeled basic protein was IgM at the peak primary response and IgG late in the response after a second immunization. There was good correlation between the results of two methods for detecting this antibody, namely, radioimmunoassay and indirect immunofluorescence using unfixed frozen sections of rabbit central nervous tissues. Fluorescence with anti-basic protein serum was specific for the basic protein and occurred predominantly in areas containing myelinated fibers. The speckled pattern contrasted with the more diffuse pattern given by an anti-myelin serum, suggesting restricted exposure of the antigenic determinants of the basic protein in the intact central nervous system. Following immunization, more than 85% of guinea pigs had measurable levels of antibody that were correlated with time after immunization, but not with immunizing quantity of basic protein. In the Lewis rat, the serum antibody level and severity of clinical signs of experimental autoimmune encephalomyelitis (EAE) were proportional to the quantity of basic protein. The lowest quantity induced clinical and histologic EAE but no measurable antibody. There was no clear correlation between presence or levels of antibody to basic protein and neurologic disease in any of the species studied. The determinant(s) of the basic protein molecule that induce antibody production, as yet not identified, were apparently not in the same region of the molecule as the main encephalitogenic determinant.

Footnotes

¹ This work was supported by grants from the National Health and Medical Research Council of Australia and the National Multiple Sclerosis Society, New York (Grant 709-A-1) and by an equipment grant for radioimmunoassay from the Multiple Sclerosis Society of Great Britain and Northern Ireland.

² This is Publication 1501 from The Walter and Eliza Hall Institute of Medical Research.

³ Clinical Research Unit, The Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, 3050, Australia.

⁴ Russell Grimwade School of Biochemistry, University of Melbourne, Victoria, 3052, Australia.

⁵ Present address: Department of Medicine, University of Alberta, Edmonton, Canada.