Galectin-Glycan Interactions as Regulators of B Cell Immunity

Front Immunol. 2018 Dec 4:9:2839. doi: 10.3389/fimmu.2018.02839. eCollection 2018.

Abstract

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.

Keywords: B cell activation; B cell receptor; B cells; GCNT2; I-antigen; I-branch; galectin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • B-Lymphocytes / immunology*
  • Galectins / immunology*
  • Glycosylation
  • Humans
  • Immunity / immunology*
  • Polysaccharides / immunology*
  • Protein Binding / immunology*
  • Signal Transduction / immunology

Substances

  • Galectins
  • Polysaccharides