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Recombinant Adenovirus Coexpressing Covalent Peptide/MHC Class II Complex and B7-1: In Vitro and In Vivo Activation of Myelin Basic Protein-Specific T Cells¹

Jiang Chen^*, Brigitte T. Huber, Richard J. Grand and Wei Li^2,*,

^* Division of Rheumatology and Immunology, Department of Pediatrics, and Center for Gastroenterology Research on Absorptive and Secretory Processes, Tufts University School of Medicine and New England Medical Center, and Immunology Program, Department of Pathology, Tufts University School of Medicine, Boston, MA 02111

Previous studies have demonstrated that an MHC class II molecule with an antigenic peptide genetically fused to its -chain is capable of presenting this peptide to CD4⁺ T cells. We hypothesized that covalent peptide/class II complex may direct the accessory molecules to exert their function specifically onto T cells in a TCR-guided fashion. To test this hypothesis, we generated several recombinant adenoviruses expressing covalent myelin basic protein peptide/I-A^u complex (MBP_1–11/I-A^u) and the costimulatory molecule B7-1. Functional studies demonstrated that adenovirus-infected cells are capable of activating an MBP_1–11-specific T cell hybridoma. Coexpression of the B7-1 molecule and MBP_1–11/I-A^u by the same adenovirus leads to synergy in T cell activation elicited by virus-infected cells. Furthermore, studies in syngeneic mice infected with the various adenoviruses revealed that MBP_1–11-specific T cells are specifically activated by the coexpression of B7-1 and MBP_1–11/I-A^u in vivo. In conclusion, the coexpression of the covalent peptide/class II complex and accessory molecules by the same adenovirus provides a unique strategy to modulate the epitope-specific T cell response in a TCR-guided fashion. This approach may be applicable to investigate the roles of other accessory molecules in the engagement of the TCR class II molecule by substituting B7-1 with other accessory molecules in the recombinant adenovirus.

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