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AssigneeThe Johns Hopkins University
InventorsJonathan Schneck, Drew Pardoll, Sean O'Herrin, Jill Slansky, Tim Greten
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To increase the effective affinity of soluble analogs of peptide/MHC molecules for their cognate ligands, divalent peptide/MHC complexes were constructed. Using a recombinant DNA strategy, DNA encoding the MHC class I was ligated to DNA coding for murine Ig heavy chain. MHC/Ig complexes were exploited to homogeneously load with peptides of interest. The results of flow cytometry demonstrated that the pepMHC/Ig complexes bound specifically with high affinity to cells bearing their cognate receptors. pepMHC/Ig complexes are also useful in modulating effector functions of antigen-specific T cells. These pepMHC/Ig complexes are useful for studying TCR/MHC interactions and lymphocyte tracking and have uses as specific regulators of immune responses.
A composition comprising at least two chimeric proteins, wherein each chimeric protein comprises an MHC molecule and an immunoglobulin chain, wherein the immunoglobulin chain of a first chimeric protein associates with the immunoglobulin chain of a second chimeric protein to form molecular complexes comprising at least two chimeric proteins per complex, wherein an antigenic peptide is bound to each MHC molecule, wherein each MHC molecule within the molecular complex is bound to an identical antigenic peptide.
A composition comprising at least two chimeric proteins, wherein each chimeric protein comprises an MHC molecule and an immunoglobulin chain, wherein the immunoglobulin chain of a first chimeric protein associates with the immunoglobulin of a second chimeric protein to form a molecular complex comprising at least two chimeric proteins per complex, wherein the immunoglobulin chain is not an IgG heavy chain.
Dependencies are inferred from the claim text.