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The MHC Class II Molecule I-A^g7 Exists in Alternate Conformations That Are Peptide Dependent¹

Department of Pathology, Committee on Immunology and Cancer Biology, University of Chicago, Chicago, IL 60637

Insulin-dependent diabetes mellitus is an autoimmune disease that is genetically linked to the HLA class II molecule DQ in humans and to MHC I-A^g7 in nonobese diabetic mice. The I-A^g7 ß-chain is unique and contains multiple polymorphisms, at least one of which is shared with DQ alleles linked to insulin-dependent diabetes mellitus. This polymorphism occurs at position 57 in the ß-chain, in which aspartic acid is mutated to a serine, a change that results in the loss of an interchain salt bridge between Arg⁷⁶ and ßAsp⁵⁷ at the periphery of the peptide binding groove. Using mAbs we have identified alternative conformations of I-A^g7 class II molecules. By using an invariant chain construct with various peptides engineered into the class II-associated invariant chain peptide (CLIP) region we have found that formation of these conformations is dependent on the peptide occupying the binding groove. Blocking studies with these Abs indicate that these conformations are present at the cell surface and are capable of interactions with TCRs that result in T cell activation.

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