LFA-1/ICAM-1 interaction lowers the threshold of B cell activation by facilitating B cell adhesion and synapse formation

Immunity. 2004 May;20(5):589-99. doi: 10.1016/s1074-7613(04)00105-0.

Abstract

The integrin LFA-1 and its ligand ICAM-1 mediate B cell adhesion, but their role in membrane-bound antigen recognition is still unknown. Here, using planar lipid bilayers and cells expressing ICAM-1 fused to green fluorescence protein, we found that the engagement of B cell receptor (BCR) promotes B cell adhesion by an LFA-1-mediated mechanism. LFA-1 is recruited to form a mature B cell synapse segregating into a ring around the BCR. This distribution is maintained over a wide range of BCR/antigen affinities (10(6) M(-1) to 10(11) M(-1)). Furthermore, the LFA-1 binding to ICAM-1 reduces the level of antigen required to form the synapse and trigger a B cell. Thus, LFA-1/ICAM-1 interaction lowers the threshold for B cell activation by promoting B cell adhesion and synapse formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • B-Lymphocytes / immunology*
  • Cell Adhesion / immunology
  • Intercellular Adhesion Molecule-1 / immunology*
  • Lipid Bilayers
  • Lymphocyte Activation / immunology*
  • Lymphocyte Function-Associated Antigen-1 / immunology*
  • Mice
  • Mice, Transgenic
  • Microscopy, Confocal
  • Polymerase Chain Reaction
  • Receptors, Antigen, B-Cell

Substances

  • Lipid Bilayers
  • Lymphocyte Function-Associated Antigen-1
  • Receptors, Antigen, B-Cell
  • Intercellular Adhesion Molecule-1