Rodak Aleksandra, Stadlmayr Gerhard, Stadlbauer Katharina, Lichtscheidl Dominic, Bobbili Madhusudhan Reddy, Rüker Florian, Wozniak-Knopp Gordana
Institute of Molecular Biotechnology, Department of Biotechnology, University of Natural Resources and Life Sciences, Vienna (BOKU), Muthgasse 18, 1190 Vienna, Austria.
Ludwig Boltzmann Institute for Experimental, Clinical Traumatology in the AUVA Research Center, Donaueschingenstrasse 13, 1200 Vienna, Austria.
Biomedicines. 2021 Oct 29;9(11):1568. doi: 10.3390/biomedicines9111568.
The increased incidence of allergies and asthma has sparked interest in IgE, the central player in the allergic response. Interaction with its high-affinity receptor FcεRI leads to sensitization and allergen presentation, extracellular membrane-proximal domain in membrane IgE can act as an antigen receptor on B cells, and the interaction with low-affinity IgE receptor CD23 additionally influences its homeostatic range. Therapeutic anti-IgE antibodies act by the inhibition of IgE functions by interfering with its receptor binding or by the obliteration of IgE-B cells, causing a reduction of serum IgE levels. Fusion proteins of antibody fragments that can act as bispecific T-cell engagers have proven very potent in eliciting cytotoxic T-lymphocyte-mediated killing. We have tested five anti-IgE Fc antibodies, recognizing different epitopes on the membrane-expressed IgE, for the ability to elicit specific T-cell activation when expressed as single-chain Fv fragments fused with anti-CD3ε single-chain antibody. All candidates could specifically stain the cell line, expressing the membrane-bound IgE-Fc and bind to CD3-positive Jurkat cells, and the specific activation of engineered CD3-overexpressing Jurkat cells and non-stimulated CD8-positive cells was demonstrated for 8D6- and ligelizumab-based bispecific antibodies. Thus, such anti-IgE antibodies have the potential to be developed into agents that reduce the serum IgE concentration by lowering the numbers of IgE-secreting cells.
过敏和哮喘发病率的上升引发了人们对IgE的兴趣,IgE是过敏反应的核心参与者。与高亲和力受体FcεRI相互作用会导致致敏和过敏原呈递,膜IgE中的细胞外膜近端结构域可作为B细胞上的抗原受体,与低亲和力IgE受体CD23的相互作用还会影响其稳态范围。治疗性抗IgE抗体通过干扰其受体结合或消除IgE-B细胞来抑制IgE功能,从而降低血清IgE水平。可作为双特异性T细胞衔接子的抗体片段融合蛋白在引发细胞毒性T淋巴细胞介导的杀伤方面已被证明非常有效。我们测试了五种抗IgE Fc抗体,它们识别膜表达IgE上的不同表位,当作为与抗CD3ε单链抗体融合的单链Fv片段表达时,测试其引发特异性T细胞活化的能力。所有候选抗体都能特异性地标记表达膜结合IgE-Fc的细胞系,并与CD3阳性的Jurkat细胞结合,基于8D6和利吉珠单抗的双特异性抗体对工程化过表达CD3的Jurkat细胞和未刺激的CD8阳性细胞具有特异性活化作用。因此,此类抗IgE抗体有潜力被开发成通过减少IgE分泌细胞数量来降低血清IgE浓度的药物。