Galectin-Glycan Interactions as Regulators of B Cell Immunity

Frontiers in Immunology

Bebhinn Treanor¹  Logan K. Smith³  Nicholas Giovannone⁴  Charles J. Dimitroff⁴ 

[1] Department of Biological Sciences, University of Toronto Scarborough, Toronto, ON, Canada;Department of Dermatology, Brigham and Women's Hospital, Boston, MA, United States;Department of Immunology, University of Toronto, Toronto, ON, Canada;Harvard Medical School, Boston, MA, United States;

关键词: B cells;    B cell activation;    B cell receptor;    galectin;    I-branch;    I-antigen;   

DOI  :  10.3389/fimmu.2018.02839

来源: DOAJ

【 摘 要 】

Cell surface glycans and their glycan-binding partners (lectins) have generally been recognized as adhesive assemblies with neighbor cells or matrix scaffolds in organs and the blood stream. However, our understanding of the roles for glycan-lectin interactions in immunity has expanded substantially to include regulation of nearly every stage of an immune response, from pathogen sensing to immune contraction. In this Mini-Review, we discuss the role of the ß-galactoside-binding lectins known as galectins specifically in the regulation of B-lymphocyte (B cell) development, activation, and differentiation. In particular, we highlight several recent studies revealing new roles for galectin (Gal)-9 in the modulation of B cell receptor-mediated signaling and activation in mouse and man. The roles for cell surface glycosylation, especially I-branching of N-glycans synthesized by the glycosyltransferase GCNT2, in the regulation of Gal-9 binding activity are also detailed. Finally, we consider how dysregulation of these factors may contribute to aberrant immune activation and autoimmune disease.

【 授权许可】

Unknown