Stabilizing mutations increase secretion of functional soluble TCR-Ig fusion proteins |
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Authors: | Elin Lunde Geir Åge Løset Bjarne Bogen Inger Sandlie |
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Affiliation: | (1) Centre for Immune Regulation, Norway;(2) Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway;(3) Institute of Immunology, University of Oslo and Oslo University Hospital, 0027 Oslo, Norway |
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Abstract: | Background Whereas T cell receptors (TCRs) detect peptide/major histocompatibility complexes (pMHCs) with exquisite specificity, there are challenges regarding their expression and use as soluble detection molecules due to molecular instability. We have investigated strategies for the production of TCR-immunoglobulin (Ig) fusion proteins. Two different TCRs that are characteristic of a mouse model for idiotype (Id) dependent immune regulation were engineered. They are structurally unrelated with different variable (V), diversity (D) and joining (J) segments, but each share one V gene segment, either Vα or Vβ, with the well characterized murine TCR, 2C. |
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