Mackin Samantha R, Sariol Alan, Diamond Michael S
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.
Department of Pathology & Immunology and Center for Genome Sciences, Lab & Genomic Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.
Immunol Rev. 2024 Nov;328(1):205-220. doi: 10.1111/imr.13383. Epub 2024 Aug 20.
Antibodies generated after vaccination or natural pathogen exposure are essential mediators of protection against many infections. Most studies with viruses have focused on antibody neutralization, in which protection is conferred by the fragment antigen binding region (Fab) through targeting of different steps in the viral lifecycle including attachment, internalization, fusion, and egress. Beyond neutralization, the fragment crystallizable (Fc) region of antibodies can integrate innate and adaptive immune responses by engaging complement components and distinct Fc gamma receptors (FcγR) on different host immune cells. In this review, we discuss recent advances in our understanding of antibody neutralization and Fc effector functions, and the assays used to measure them. Additionally, we describe the contexts in which these mechanisms are associated with protection against viruses and highlight how Fc-FcγR interactions can improve the potency of antibody-based therapies.
接种疫苗或自然接触病原体后产生的抗体是抵御多种感染的重要保护介质。大多数针对病毒的研究都集中在抗体中和作用上,即通过片段抗原结合区(Fab)靶向病毒生命周期中的不同步骤(包括附着、内化、融合和释放)来提供保护。除了中和作用外,抗体的可结晶片段(Fc)区域可通过与补体成分以及不同宿主免疫细胞上不同的Fcγ受体(FcγR)结合,整合先天性和适应性免疫反应。在这篇综述中,我们讨论了我们对抗体中和作用和Fc效应功能的理解方面的最新进展,以及用于测量它们的检测方法。此外,我们描述了这些机制与抗病毒保护相关的背景,并强调了Fc-FcγR相互作用如何提高基于抗体的治疗效力。