Yu Hui-Chun, Huang Kuang-Yung, Lu Ming-Chi, Huang Hsien-Lu, Liu Wei-Ting, Lee Wen-Chien, Liu Su-Qin, Huang Hsien-Bin, Lai Ning-Sheng
Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan.
Section of Allergy, Immunology and Rheumatology, Department of Medicine, Buddhist DaLin Tzu-Chi Hospital, Chia-Yi 622, Taiwan.
Int J Mol Sci. 2015 Apr 13;16(4):8142-50. doi: 10.3390/ijms16048142.
BH2, a monoclonal antibody prepared against the denatured human leukocytic antigen-B27 heavy chain (HLA-B27 HC), can immunoprecipitate the misfolded HLA-B27 HC complexed with Bip in the endoplasmic reticulum and recognize the homodimerized HLA-B27 HC that is often observed on the cell membrane of patients suffered from ankylosing spondylitis (AS). However, the recognition specificity of BH2 toward the other molecules of HLA-B type and toward the different types of HLA molecules remained uncharacterized. In this study, we carried out the HLA-typing by using the Luminex Technology to characterize the recognition specificity of BH2 and analyzed the binding domain of HLA-B27 HC by BH2. Our results indicated that BH2 preferably binds to molecules of HLA-B and -C rather than HLA-A and the binding site is located within the α2 domain of HLA-B27 HC.
BH2是一种针对变性人白细胞抗原B27重链(HLA - B27 HC)制备的单克隆抗体,它能免疫沉淀在内质网中与Bip复合的错误折叠的HLA - B27 HC,并识别在强直性脊柱炎(AS)患者细胞膜上经常观察到的同型二聚化的HLA - B27 HC。然而,BH2对其他HLA - B型分子以及不同类型HLA分子的识别特异性仍未明确。在本研究中,我们使用Luminex技术进行HLA分型以表征BH2的识别特异性,并通过BH2分析HLA - B27 HC的结合域。我们的结果表明,BH2优先结合HLA - B和 - C分子而非HLA - A分子,且结合位点位于HLA - B27 HC的α2结构域内。