Reinhart David, Kunert Renate
Department of Biotechnology, Vienna Institute of BioTechnology, University of Natural Resources and Life Sciences, Muthgasse 11, 1190, Vienna, Austria,
Biotechnol Lett. 2015 Feb;37(2):241-51. doi: 10.1007/s10529-014-1686-z. Epub 2014 Sep 26.
Immunoglobulin A (IgA) is the most abundant antibody class in the human body and has a unique role in mediating immunity. The ever-increasing knowledge about the potential of IgAs has renewed interest in this antibody class for therapeutic use against a variety of infectious and malignant diseases, and as a preventive agent for mucosal pathogens. Despite the considerable therapeutic potential of IgA the exploration thereof has often been hampered due to difficulties in producing and purifying desired quantities. Large amounts of pure IgA will be required for in vivo studies. This work reviews current achievements and bottlenecks in upstream and downstream processing of recombinant IgA from a biotechnological point of view. We also highlight recent accomplishments with diverse expression systems and presents different affinity techniques for the capture of recombinant IgA to compare their purification potential.
免疫球蛋白A（IgA）是人体中含量最丰富的抗体类别，在介导免疫方面具有独特作用。关于IgA潜力的认识不断增加，这重新激发了人们对这类抗体用于治疗各种感染性和恶性疾病以及作为黏膜病原体预防剂的兴趣。尽管IgA具有相当大的治疗潜力，但由于生产和纯化所需数量存在困难，对其探索常常受到阻碍。体内研究将需要大量的纯IgA。这项工作从生物技术的角度综述了重组IgA上游和下游加工的当前成就和瓶颈。我们还强调了不同表达系统的最新成果，并介绍了用于捕获重组IgA的不同亲和技术，以比较它们的纯化潜力。
