Cutting edge: single-chain trimers of MHC class I molecules form stable structures that potently stimulate antigen-specific T cells and B cells
YYL Yu, N Netuschil, L Lybarger… - The Journal of …, 2002 - journals.aai.org
YYL Yu, N Netuschil, L Lybarger, JM Connolly, TH Hansen
The Journal of Immunology, 2002•journals.aai.orgWe report in this work the expression and characterization of class I molecules expressed as
single-chain trimers consisting of an antigenic peptide-spacer-β 2-microglobulin-spacer H
chain. Our results indicate that these single-chain constructs assemble efficiently, maintain
their covalent structure, and are unusually stable at the cell surface. Consequently, these
constructs are at least 1000-fold less accessible to exogenous peptide than class I
molecules loaded with endogenous peptides, and they are potent simulators of peptide …
single-chain trimers consisting of an antigenic peptide-spacer-β 2-microglobulin-spacer H
chain. Our results indicate that these single-chain constructs assemble efficiently, maintain
their covalent structure, and are unusually stable at the cell surface. Consequently, these
constructs are at least 1000-fold less accessible to exogenous peptide than class I
molecules loaded with endogenous peptides, and they are potent simulators of peptide …
Abstract
We report in this work the expression and characterization of class I molecules expressed as single-chain trimers consisting of an antigenic peptide-spacer-β 2-microglobulin-spacer H chain. Our results indicate that these single-chain constructs assemble efficiently, maintain their covalent structure, and are unusually stable at the cell surface. Consequently, these constructs are at least 1000-fold less accessible to exogenous peptide than class I molecules loaded with endogenous peptides, and they are potent simulators of peptide-specific CTL and Abs. Our combined findings suggest that single-chain trimers may have applications as DNA vaccines against virus infection or tumors.
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