Ge J, Bartnes K, Hannestad K
Department of Immunology, University of Tromsø, School of Medicine, Norway.
Tissue Antigens. 1993 Feb;41(2):81-5. doi: 10.1111/j.1399-0039.1993.tb01983.x.
TrJ1 is a cytotoxic human hybridoma mAb (IgM lambda). Its reaction pattern with a panel of 42 HLA-defined lymphoblastoid B-cell lines correlated precisely with expression of DQ2. By flow cytometry it was shown that the binding of TrJ1 to DQ2 was efficiently blocked by the murine anti-DQ2 mAb 358.4, indicating that the TrJ1 and 358.4 epitopes overlap. TrJ1 reacted much better with EBV-transformed B cells than with B cells freshly isolated from blood. TrJ1 seemed suitable for typing freshly isolated B cells provided the incubation with complement lasted for 115 min in Terasaki plates. One or more of the DQ2-specific polymorphic amino acids E46, F47, L52, L55, K71 or A74, situated on the alpha-helix of the DQ2 beta chain, are probably critical for the TrJ1 epitope.
TrJ1是一种具有细胞毒性的人杂交瘤单克隆抗体(IgM λ)。它与一组42个经HLA分型的淋巴母细胞样B细胞系的反应模式与DQ2的表达精确相关。通过流式细胞术表明,鼠抗-DQ2单克隆抗体358.4可有效阻断TrJ1与DQ2的结合,这表明TrJ1和358.4的表位重叠。TrJ1与EB病毒转化的B细胞的反应比与从血液中新鲜分离的B细胞的反应要好得多。如果在寺崎培养板中与补体孵育持续115分钟,TrJ1似乎适用于对新鲜分离的B细胞进行分型。位于DQ2 β链α螺旋上的一个或多个DQ2特异性多态性氨基酸E46、F47、L52、L55、K71或A74可能对TrJ1表位至关重要。