Properties of Antibodies Produced in Rabbits to Human Myelin and Myelin Basic Protein

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Abstract
The patterns of reactivity of antisera raised in rabbits to human myelin and to the basic protein of human myelin were studied by immunofluorescence, using frozen sections from autologous as well as heterologous central nervous system (CNS) and smears of myelin and a synaptosomal membrane fraction of CNS. Whole myelin induced antibodies which reacted with myelinated areas in frozen sections of the CNS in a homogeneous pattern, and with smears of myelin and the synaptosomal membrane fraction; this activity was absorbed from serum by myelin, by the water-insoluble fraction of myelin, but not by the basic protein of myelin. The basic protein of myelin induced antibodies which reacted with myelinated areas in the CNS in a finely speckled pattern, and with smears of myelin and the synaptosomal membrane fraction; this activity was absorbed from serum by myelin, by myelin basic protein and partly by histones. This evidence of cross-reactivity in immunofluorescence tests between the myelin basic protein and histones was corroborated by partial competitive inhibition between histone and the myelin basic protein in the radioimmunoassay for antibody to basic protein. An antigen similar to myelin basic protein is present in the synaptosomal membrane fraction of CNS and hence synaptosomes are potential reactive sites for the pathogenic immune response in experimental allergic encephalomyelitis.

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