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HLA-G (human leukocyte antigen-G) is a non-classical HLA class Ⅰ molecule, playing an important immuno-modulatoryrole in maintaining maternal immune tolerance of the semiallogenic fetus and organ transplantation. In this study, the cDNA sequence ofextracallular domain of HLA-G1 was subcloned into the pET28a vector and a soluble 35 kD fusion protein (His-sHLA-G1) with six histineresidues was obtained. In the 4h ~(51)Cr-release assay the fusion protein obviously inhibited the cytotoxicity of NK92 cells in a dose-depen-dent manner. These results indicated that sHLA-G1, as an activated immunoinhibitor, may provide an effective approach to overcomingthe immune rejection of transplantation.
HLA-G (human leukocyte antigen-G) is a non-classical HLA class I molecule, playing an important immuno-modulatoryrole in maintaining maternal immune tolerance of the semiallogenic fetus and organ transplantation. In this study, the cDNA sequence of extracallular domain of HLA -G1 was subcloned into the pET28a vector and a soluble 35 kD fusion protein (His-sHLA-G1) with six histine residues. In the 4h ~ (51) Cr-release assay the fusion protein obviously inhibited the cytotoxicity of NK92 cells in a dose-depen-dent manner. These results indicate that sHLA-G1, as an activated immunoinhibitor, may provide an effective approach to overcoming the immune rejection of transplantation.