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Related Experiment Videos

CD18 activation epitopes induced by leukocyte activation.

C R Beals1, A C Edwards, R J Gottschalk

  • 1ICOS, Bothell, WA 98021, USA. cbeals@icos.com

Journal of Immunology (Baltimore, Md. : 1950)
|November 21, 2001
PubMed
Summary

New antibodies reveal conformational changes in leukocyte function-associated antigen-1 (LFA-1) during T cell activation. These changes, independent of ligand binding, are crucial for immune cell trafficking and T cell responses.

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Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Leukocyte function-associated antigen-1 (LFA-1) is vital for leukocyte trafficking and T cell activation.
  • Understanding LFA-1 conformational changes is key to dissecting immune cell signaling.

Purpose of the Study:

  • To develop and characterize monoclonal antibodies (mAbs) targeting activation epitopes on the CD18 subunit of LFA-1.
  • To investigate the conformational dynamics of LFA-1 during T cell activation and its relation to adhesion and signaling.

Main Methods:

  • Development of a panel of mAbs against CD18 activation epitopes.
  • Analysis of epitope expression in response to T cell stimulation, divalent cations, and signal transduction inhibitors.
  • Assessment of epitope expression in leukocyte adhesion deficiency cell lines.

Related Experiment Videos

  • Evaluation of the impact of function-blocking CD18 antibodies on epitope induction.
  • Characterization of neoepitope binding to recombinant LFA-1 (rLFA-1) and its affinity for ICAM-1.

    • Main Results:

    • T cell stimulation induces a conformational change in a subpopulation of LFA-1, independent of ligand binding.
    • Epitope upregulation requires divalent cations and is sensitive to cellular signaling, correlating with cell adhesion.
    • Absence of epitope induction in leukocyte adhesion deficiency-1/variant cells highlights the role of LFA-1 activation.
    • Function-blocking CD18 antibodies inhibit epitope induction, suggesting they block a conformational change.
    • Neoepitopes are present on high-affinity rLFA-1 for ICAM-1, mirroring LFA-1 affinity modulation.

    Conclusions:

    • Novel CD18 activation epitope antibodies can dissect signal transmission to LFA-1.
    • These epitopes are early indicators of cellular activation, preceding actin rearrangement.
    • The identified neoepitopes mark a subpopulation of LFA-1 with high ICAM-1 affinity, essential for LFA-1 function.