Huang J H, Getty R R, Chisari F V, Fowler P, Greenspan N S, Tykocinski M L
Institute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Immunity. 1994 Oct;1(7):607-13. doi: 10.1016/1074-7613(94)90050-7.
Recombinant GPI-anchored HLA-A2.1 (HLA-A2.1-GPI/beta 2m) was used as a protein transfer vehicle to deliver a hepatitis B virus antigenic peptide to the surfaces of cytotoxic T cell targets. Empty HLA-A2.1-GPI/beta 2m was first produced in D. melanogaster cotransfectants and immunoaffinity purified. Cell coating with HLA-A2.1-GPI/beta 2m was shown to occur rapidly, and to be protein concentration dependent. Protein-transferred HLA-A2.1-GPI/beta 2m effectively presented a hepatitis B virus peptide to peptide-specific HLA-A2.1-restricted T cell clones in cytotoxicity assays. Protein transfer of functional GPI-modified class I MHC-antigenic peptide complexes represents a novel strategy for delivering functional antigenic complexes to cell surfaces that bypasses limitations of gene transfer and permits control of antigenic peptide densities at cell surfaces.
重组糖基磷脂酰肌醇（GPI）锚定的HLA - A2.1（HLA - A2.1 - GPI/β2m）被用作蛋白质转移载体，将乙肝病毒抗原肽递送至细胞毒性T细胞靶标的表面。首先在黑腹果蝇共转染细胞中产生空的HLA - A2.1 - GPI/β2m，并通过免疫亲和法进行纯化。结果表明，用HLA - A2.1 - GPI/β2m包被细胞的过程迅速，且依赖于蛋白质浓度。在细胞毒性试验中，蛋白质转移的HLA - A2.1 - GPI/β2m有效地将乙肝病毒肽呈递给肽特异性HLA - A2.1限制性T细胞克隆。功能性GPI修饰的I类主要组织相容性复合体 - 抗原肽复合物的蛋白质转移代表了一种将功能性抗原复合物递送至细胞表面的新策略，该策略绕过了基因转移的局限性，并允许控制细胞表面抗原肽的密度。
