Ohkuri Takatoshi, Yuge Natsuko, Sato Kenji, Ueda Tadashi
Graduate School of Pharmaceutical Sciences, Kyushu University, Japan.
Faculty of Pharmaceutical Sciences, Sojo University, Japan.
Biochem Biophys Rep. 2019 Aug 14;20:100679. doi: 10.1016/j.bbrep.2019.100679. eCollection 2019 Dec.
During treatment with protein therapeutics, such as monoclonal antibodies, the development of anti-drug antibodies is a serious side-effect of modern pharmacology. Anti-drug antibodies are produced as the number and exposure to therapeutic proteins increase. In this context, less immunogenic responses could diminish these noxious effects. Biophysical characterization of antigens, that is size, chemical composition, physical form, and degrability, are known to influence the outcome of immune responses. Here, using chemical modification, we have prepared oligomers of hen egg lysozyme (HEL), 3- to 5-mer, as a typical antigen in immunology and evaluated the efficacy as a tolerogen in HEL-specific antibody responses. Our results clearly demonstrated that pre-exposed the HEL-oligomers into mice effectively suppressed HEL-specific IgG responses regardless of the cross-linking mode. Therefore, the oligomerization is a method to induce tolerogenicity of proteins and may emerge as a promising strategy to control the production of undesirable anti-protein drug antibodies.
在用蛋白质疗法(如单克隆抗体)进行治疗的过程中,抗药抗体的产生是现代药理学的一个严重副作用。随着治疗性蛋白质数量的增加和暴露时间的延长,抗药抗体也会产生。在这种情况下,免疫原性较低的反应可能会减少这些有害影响。已知抗原的生物物理特性,即大小、化学成分、物理形态和可降解性,会影响免疫反应的结果。在此,我们通过化学修饰制备了3至5聚体的鸡蛋清溶菌酶(HEL)寡聚物,作为免疫学中的典型抗原,并评估了其作为耐受原在HEL特异性抗体反应中的效果。我们的结果清楚地表明,将HEL寡聚物预先暴露于小鼠体内,无论交联模式如何,都能有效抑制HEL特异性IgG反应。因此,寡聚化是一种诱导蛋白质耐受性的方法,可能会成为控制不良抗蛋白质药物抗体产生的一种有前景的策略。