The Immunoregulatory Roles of Antibody Glycosylation

被引：236

作者：

Jennewein, Madeleine F. ^{[1
]}

Alter, Galit ^{[1
]}

机构：

[1] Ragon Inst MGH MIT & Harvard, Cambridge, MA 02139 USA

来源：

TRENDS IN IMMUNOLOGY | 2017年 / 38卷 / 05期

关键词：

DEPENDENT CELLULAR CYTOTOXICITY; FC-GAMMA-RIII; SYSTEMIC-LUPUS-ERYTHEMATOSUS; CLASS-SWITCH RECOMBINATION; HIGH-AFFINITY BINDING; RHEUMATOID-ARTHRITIS; NONNEUTRALIZING ANTIBODIES; ANTIINFLAMMATORY ACTIVITY; FUNCTIONAL ANTIBODIES; N-GLYCOSYLATION;

D O I：

10.1016/j.it.2017.02.004

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Beyond their role in neutralization, antibodies mediate functions such as phagocytosis, cytotoxicity, and maintenance of immune homeostasis. Two modifications to the constant domain control antibody activity: theirreversible genomic selection of isotype/subclass and alterations in glycosylation. Because glycosylation alters the affinity of antibodies for Fc receptors, evidence suggests that glycosylation is a central mechanism for the immune system to tune a broad range of biological activities. While monoclonal therapeutics have exploited glycosylation to improve function, its in vivo control and whether it may be selectively harnessed to target pathogens and/or tumors is unknown. Here, we review the process of antibody glycosylation, how it changes with disease, how it impacts antibody functionality, and the potential for deliberately controlling this biological activity.

引用

页码：358 / 372

页数：15

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