Characterization of the Recognition Specificity of BH2, a Monoclonal Antibody Prepared against the HLA-B27 Heavy Chain

International Journal of Molecular Sciences

Hui-Chun Yu²  Kuang-Yung Huang²  Ming-Chi Lu¹  Hsien-Lu Huang³  Wei-Ting Liu²  Wen-Chien Lee⁴  Su-Qin Liu¹  Hsien-Bin Huang²  Ning-Sheng Lai¹ 

[1] Section of Allergy, Immunology and Rheumatology, Department of Medicine, Buddhist DaLin Tzu-Chi Hospital, Chia-Yi 622, Taiwan; E-Mails:;Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan; E-Mails:;Department of Nutrition and Health Science, Fooyin University, Kaohsiung 831, Taiwan; E-Mail:;Department of Chemical Engineering, National Chung Cheng University, Chia-Yi 621, Taiwan; E-Mail:

关键词: HLA-B27;    ankylosing spondylitis;    monoclonal antibody;    HLA-typing;   

DOI  :  10.3390/ijms16048142

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.