Abstract

Acetylated peptide 1-9 from human myelin basic protein induces experimental allergic encephalomyelitis in PL/J mice through I-Au and TCR V beta 8.2. Murine mAb anti-Id directed against murine mAb to myelin basic protein peptide acetyl 1-9 was examined for effects on in vitro and in vivo T cell activities. Certain anti-Id, generated in PL/J mice, inhibited Ag-specific proliferation and IL-2 production and precipitated surface receptors having features of the TCR. The idiotypic features of TCR recognition were demonstrated by showing that binding of anti-Id to the TCR could be blocked by anti-TCR alpha beta and anti-TCR V beta 8.1-8.2 but not by murine Ig or anti-TCR V beta 17a. In addition, the anti-Id did not react with TCR V beta 8.2 transgenically inserted into MRL+/+ mice. One anti-Id was also capable of lessening clinical disease activity in the adoptive passive transfer model of experimental allergic encephalomyelitis in PL/J mice. These results indicate that anti-Id may recognize a cross-reactive Id on T cells, presumably on the TCR, responsive to the same I-Au-restricted encephalitogenic myelin basic protein peptide in PL/J mice. The selective development of anti-Id and their effect on T cell-mediated tissue damage provide a method for applying specific anti-Id antibodies to modify experimental and, possibly, spontaneous diseases of autoimmune demyelination.