Office of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
MAbs. 2024 Jan-Dec;16(1):2304268. doi: 10.1080/19420862.2024.2304268. Epub 2024 Jan 22.
Glycosylation plays a crucial role in determining the quality and efficacy of therapeutic antibodies. This necessitates a thorough analysis and monitoring process to ensure consistent product quality during manufacturing. In this study, we introduce a custom-designed lectin microarray featuring nine distinct lectins: rPhoSL, rOTH3, RCA120, rMan2, MAL_I, rPSL1a, PHAE, rMOA, and PHAL. These lectins have been specifically tailored to selectively bind to common N-glycan epitopes found in therapeutic IgG antibodies. By utilizing intact glycoprotein samples, our nine-lectin microarray provides a high-throughput platform for rapid glycan profiling, enabling comparative analysis of glycosylation patterns. Our results demonstrate the practical utility of this microarray in assessing glycosylation across various manufacturing batches or between biosimilar and innovator products. This capacity empowers informed decision-making in the development and production of therapeutic antibodies.
糖基化在决定治疗性抗体的质量和疗效方面起着至关重要的作用。这需要进行彻底的分析和监测过程，以确保在制造过程中始终如一的产品质量。在这项研究中，我们引入了一种定制设计的凝集素微阵列，其中包含九种独特的凝集素：rPhoSL、rOTH3、RCA120、rMan2、MAL_I、rPSL1a、PHAE、rMOA 和 PHAL。这些凝集素经过专门设计，能够选择性地结合治疗性 IgG 抗体中常见的 N-糖基化表位。通过使用完整的糖蛋白样品，我们的九种凝集素微阵列提供了一种高通量的聚糖分析平台，能够进行糖基化模式的比较分析。我们的结果表明，该微阵列在评估各种制造批次之间或生物类似药和创新药产品之间的糖基化方面具有实际应用价值。这种能力为治疗性抗体的开发和生产提供了明智决策的能力。
