Department of Clinical Research, National Hospital Organization Yamaguchi Ube Medical Center, Ube, Japan.
NIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Mount Merrion, Blackrock, Co Dublin, Ireland.
Exp Suppl. 2021;112:1-26. doi: 10.1007/978-3-030-76912-3_1.
Therapeutic monoclonal antibodies (mAbs) are mostly of the IgG class and constitute highly efficacious biopharmaceuticals for a wide range of clinical indications. Full-length IgG mAbs are large proteins that are subject to multiple posttranslational modifications (PTMs) during biosynthesis, purification, or storage, resulting in micro-heterogeneity. The production of recombinant mAbs in nonhuman cell lines may result in loss of structural fidelity and the generation of variants having altered stability, biological activities, and/or immunogenic potential. Additionally, even fully human therapeutic mAbs are of unique specificity, by design, and, consequently, of unique structure; therefore, structural elements may be recognized as non-self by individuals within an outbred human population to provoke an anti-therapeutic/anti-drug antibody (ATA/ADA) response. Consequently, regulatory authorities require that the structure of a potential mAb drug product is comprehensively characterized employing state-of-the-art orthogonal analytical technologies; the PTM profile may define a set of critical quality attributes (CQAs) for the drug product that must be maintained, employing quality by design parameters, throughout the lifetime of the drug. Glycosylation of IgG-Fc, at Asn297 on each heavy chain, is an established CQA since its presence and fine structure can have a profound impact on efficacy and safety. The glycoform profile of serum-derived IgG is highly heterogeneous while mAbs produced in mammalian cells in vitro is less heterogeneous and can be "orchestrated" depending on the cell line employed and the culture conditions adopted. Thus, the gross structure and PTM profile of a given mAb, established for the drug substance gaining regulatory approval, have to be maintained for the lifespan of the drug. This review outlines our current understanding of common PTMs detected in mAbs and endogenous IgG and the relationship between a variant's structural attribute and its impact on clinical performance.
治疗性单克隆抗体(mAbs)大多属于 IgG 类,是广泛临床适应证的高效生物制药。全长 IgG mAbs 是大型蛋白质,在生物合成、纯化或储存过程中会发生多种翻译后修饰(PTMs),导致微异质性。在非人类细胞系中生产重组 mAbs 可能导致结构保真度丧失,并产生稳定性、生物活性和/或免疫原性改变的变体。此外,即使是完全人源的治疗性 mAbs 也具有独特的特异性,因此具有独特的结构;因此,结构元素可能会被外群人群中的个体识别为非自身,从而引发抗治疗/抗药物抗体(ATA/ADA)反应。因此,监管机构要求潜在 mAb 药物产品的结构采用最先进的正交分析技术进行全面表征;PTM 谱可确定药物产品的一组关键质量属性(CQAs),必须通过质量源于设计参数在药物的整个生命周期内保持。每个重链上 Asn297 的 IgG-Fc 糖基化是一个已建立的 CQA,因为其存在和精细结构会对疗效和安全性产生深远影响。血清衍生 IgG 的糖型谱高度异质,而体外哺乳动物细胞生产的 mAbs 则异质性较低,并且可以根据所使用的细胞系和采用的培养条件进行“协调”。因此,获得监管批准的药物物质的给定 mAb 的总结构和 PTM 谱必须在药物的整个生命周期内保持。本文综述了我们对 mAbs 和内源性 IgG 中常见 PTM 的理解,以及变体结构属性与其临床性能之间的关系。