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,
,§
*
Neuroimmunology Research, Veterans Affairs Medical Center, Portland, OR 97201; and
Department of Neurology,
Department of Biochemistry and Molecular Biology, and
§
Department of Molecular Microbiology and Immunology, Oregon Health Sciences University, Portland, OR 97201
We designed and expressed in bacteria a single-chain two-domain MHC
class II molecule capable of binding and forming stable complexes with
antigenic peptide. The prototype "ß1
1"
molecule included the ß1 domain of the rat RT1.B class II
molecule covalently linked to the amino terminus of the
1 domain. In association with the encephalitogenic
myelin basic protein (MBP) 69–89 peptide recognized by Lewis rat T
cells, the ß11/MBP-69–89 complex
specifically labeled and inhibited activation of MBP-69–89 reactive T
cells in an IL-2-reversible manner. Moreover, this complex both
suppressed and treated clinical signs of experimental autoimmune
encephalomyelitis and inhibited delayed-type hypersensitivity reactions
and lymphocyte proliferation in an Ag-specific manner. These data
indicate that the ß11/MBP-69–89 complex
functions as a simplified natural TCR ligand with potent inhibitory
activity that does not require additional signaling from the
ß2 and 2 domains. This new class of small
soluble polypeptide may provide a template for designing human
homologues useful in detecting and regulating potentially
autopathogenic T cells.
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