Journal
CHEMISTRY & BIOLOGY
Volume 14, Issue 8, Pages 909-922Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2007.07.010
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Funding
- NIAID NIH HHS [AI055849, AI27568, R01 AI019687, U54-AI057160, R56 AI055849, R01 AI055849, R01 AI027568, AI5142604] Funding Source: Medline
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MHC class I pepticle complexes (pMHC) are routinely used to enumerate T cell populations and are currently being evaluated as vaccines to tumors and specific pathogens. Herein, we describe the structures of three generations of single-chain pMHC progressively designed for the optimal presentation of covalently associated epitopes. Our ultimate design employs a versatile disulfide trap between an invariant MHC residue and a short C-terminal pepticle extension. This general strategy is nondisruptive of native pMHC conformation and T cell receptorengagement. Indeed, cell-surface-expressed MHC complexes with disulfide-trapped epitopes are refractory to peptide exchange, suggesting they will make safe and effective vaccines. Furthermore, we find that disulfide-trap stabilized, recombinant pMHC reagents reliably detect polyclonal CD8 T cell populations as proficiently as conventional reagents and are thus well suited to monitor or modulate immune responses during pathogenesis.
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