Mutated HLA-G3 localizes to the cell surface but does not inhibit cytotoxicity of natural killer cells |
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Authors: | Longmei Zhao Takele TeklemariamBasil M Hantash |
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Institution: | Escape Therapeutics, Inc., San Jose, CA, United States |
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Abstract: | HLA-G plays an important role in the induction of immune tolerance. Various attempts to produce good manufacturing practice levels of HLA-G as a therapeutic molecule have failed to date partly due to the complicated structure of full-length HLA-G1. Truncated HLA-G3 is simpler and easier to produce than HLA-G1 and contains the expected functional epitope in its only α1 monomorphic domain. In this study, we engineered the ER retrieval and retention signal on HLA-G3’s cytoplasmic tail by replacing its RKKSSD motif with RAASSD. We observed that mutated HLA-G3 was highly expressed on the cell surface of transduced K562 cells but did not inhibit cytotoxicity of natural killer cells. |
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Keywords: | HLA-G3 Mutation Cell surface expression Cytotoxicity Natural killer cell |
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