The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion

Nature. 1990 May 3;345(6270):74-7. doi: 10.1038/345074a0.

Abstract

Interaction with antigen-presenting accessory cells is thought to be an important step in B-cell activation, and the B-cell receptor CD22, which is coordinately expressed with surface immunoglobulin, has been proposed to participate in the antigen response. Here we show that CD22 has a structure closely related to myelin-associated glycoprotein (MAG, a neuronal adhesion protein), and mediates monocyte and erythrocyte adhesion. Like CD2, the T-cell erythrocyte receptor, CD22 may facilitate antigen recognition by promoting antigen-nonspecific contacts with accessory cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD / genetics
  • Antigens, CD / immunology*
  • Antigens, Differentiation, B-Lymphocyte / genetics
  • Antigens, Differentiation, B-Lymphocyte / immunology*
  • B-Lymphocytes / immunology*
  • Base Sequence
  • Cell Adhesion / immunology
  • Cell Adhesion Molecules*
  • Cloning, Molecular
  • Erythrocytes / immunology*
  • Immunosorbent Techniques
  • Lectins*
  • Molecular Sequence Data
  • Molecular Weight
  • Monocytes / immunology*
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Nucleic Acid Hybridization
  • RNA / analysis
  • Receptors, Antigen, B-Cell / immunology
  • Recombinant Proteins / immunology
  • Rosette Formation
  • Sequence Homology, Nucleic Acid
  • Sialic Acid Binding Ig-like Lectin 2
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • Cell Adhesion Molecules
  • Lectins
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Receptors, Antigen, B-Cell
  • Recombinant Proteins
  • Sialic Acid Binding Ig-like Lectin 2
  • RNA