Department of Tropical Disease Biology, Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool, UK.
MAbs. 2021 Jan-Dec;13(1):1953220. doi: 10.1080/19420862.2021.1953220.
Pathogens frequently use multivalent binding to sialic acid to infect cells or to modulate immunity through interactions with human sialic acid-binding immunoglobulin-type lectins (Siglecs). Molecules that interfere with these interactions could be of interest as diagnostics, anti-infectives or as immune modulators. This review describes the development of molecular scaffolds based on the crystallizable fragment (Fc) region of immunoglobulin (Ig) G that deliver high-avidity binding to innate immune receptors, including sialic acid-dependent receptors. The ways in which the sialylated Fc may be engineered as immune modulators that mimic the anti-inflammatory properties of intravenous polyclonal Ig or as blockers of sialic-acid-dependent infectivity by viruses are also discussed.
病原体经常利用多价结合唾液酸来感染细胞，或通过与人类唾液酸结合免疫球蛋白型凝集素（Siglecs）相互作用来调节免疫。干扰这些相互作用的分子可能作为诊断试剂、抗感染药物或免疫调节剂而受到关注。本文综述了基于免疫球蛋白（Ig）G 的可结晶片段（Fc）区域的分子支架的开发，这些支架可高亲和力结合先天免疫受体，包括依赖唾液酸的受体。还讨论了如何将唾液酸化的 Fc 工程化为模拟静脉注射多克隆 Ig 的抗炎特性的免疫调节剂，或作为病毒依赖唾液酸的感染力的阻断剂。
