IgG Fab糖基化在免疫中的新重要性。

The Emerging Importance of IgG Fab Glycosylation in Immunity.

作者信息

van de Bovenkamp Fleur S, Hafkenscheid Lise, Rispens Theo, Rombouts Yoann

机构信息

Department of Immunopathology, Sanquin Research, 1066 CX Amsterdam, the Netherlands; Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, 1105 AZ Amsterdam, the Netherlands;

Department of Rheumatology, Leiden University Medical Center, 2333 ZA Leiden, the Netherlands;

出版信息

J Immunol. 2016 Feb 15;196(4):1435-41. doi: 10.4049/jimmunol.1502136.

DOI:10.4049/jimmunol.1502136

PMID:26851295

Abstract

Human IgG is the most abundant glycoprotein in serum and is crucial for protective immunity. In addition to conserved IgG Fc glycans, ∼15-25% of serum IgG contains glycans within the variable domains. These so-called "Fab glycans" are primarily highly processed complex-type biantennary N-glycans linked to N-glycosylation sites that emerge during somatic hypermutation. Specific patterns of Fab glycosylation are concurrent with physiological and pathological conditions, such as pregnancy and rheumatoid arthritis. With respect to function, Fab glycosylation can significantly affect stability, half-life, and binding characteristics of Abs and BCRs. Moreover, Fab glycans are associated with the anti-inflammatory activity of IVIgs. Consequently, IgG Fab glycosylation appears to be an important, yet poorly understood, process that modulates immunity.

摘要

人IgG是血清中最丰富的糖蛋白，对保护性免疫至关重要。除了保守的IgG Fc聚糖外，约15 - 25%的血清IgG在可变区内含有聚糖。这些所谓的“Fab聚糖”主要是高度加工的复合型双天线N - 聚糖，与体细胞超突变过程中出现的N - 糖基化位点相连。Fab糖基化的特定模式与生理和病理状况相关，如妊娠和类风湿性关节炎。在功能方面，Fab糖基化可显著影响抗体和BCR的稳定性、半衰期及结合特性。此外，Fab聚糖与静脉注射免疫球蛋白的抗炎活性相关。因此，IgG Fab糖基化似乎是一个重要但尚未被充分理解的调节免疫的过程。