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• W2122321884 endingPage "916" @default.
• W2122321884 startingPage "902" @default.
• W2122321884 abstract "The variable (V) domains of antibodies and T cell receptors (TCRs) share sequence homology and striking structural similarity. Single-chain antibody V domain constructs (scFv) are routinely expressed in a variety of heterologous systems, both for production of soluble protein as well as for in vitro engineering. In contrast, single-chain T cell receptor V domain constructs (scTCR) are prone to aggregation and misfolding and are refractory to display on phage or yeast in their wild-type form. However, through random mutagenesis and yeast display engineering, it has been possible to isolate scTCR mutants that are properly folded and displayed on the yeast surface. These displayed mutants can serve not only as a scaffold for further engineering but also as scTCR variants that exhibit favorable biophysical properties in Escherichia coli expression. Thus, a more comprehensive understanding of the V domain mutations that allowed display would be beneficial. Our goal here was to identify generalizable patterns of important mutations that can be applied to different TCRs. We compared five different scTCRs, four from mice and one from a human, for yeast surface display. Analysis of a collection of mutants revealed four distinct regions of TCR V domains that were most important for enabling surface expression: the Valpha-Vbeta interface, the HV4 of Vbeta, and the region of the Valpha and Vbeta domains normally apposed against the constant (C) domains. Consistent with the role of the V-C interface in surface display, reconstitution of this interface, by including the constant domains of each chain, allowed V domain display and alphabeta chain association on the yeast surface, thus providing an alternative TCR scaffold. However, the surface levels of TCR achieved with engineered scTCR mutants were superior to that of the ValphaCalpha/VbetaCbeta constructs. Therefore, we describe further optimization of the current strategy for surface display of the single-chain format in order to facilitate yeast display engineering of a broader range of scTCRs." @default.
• W2122321884 created "2016-06-24" @default.
• W2122321884 creator A5023806324 @default.
• W2122321884 creator A5030463228 @default.
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• W2122321884 date "2009-02-01" @default.
• W2122321884 modified "2023-10-14" @default.
• W2122321884 title "Structural features of T cell receptor variable regions that enhance domain stability and enable expression as single-chain VαVβ fragments" @default.
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• W2122321884 doi "https://doi.org/10.1016/j.molimm.2008.09.021" @default.
• W2122321884 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2666936" @default.
• W2122321884 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18962897" @default.
• W2122321884 hasPublicationYear "2009" @default.
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