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A distinct cytoplasmic domain of CD2 regulates ligand avidity and T-cell responsiveness to antigen

W C Hahn1, Y Rosenstein, V Calvo

  • 1Division of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 1992
PubMed

Insights

T-cell receptor signaling enhances CD2 binding to CD58, boosting T-cell activation. This adhesion strengthening, independent of CD2 signaling, is crucial for antigen-specific responses.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • CD2 is a T-cell glycoprotein involved in cell adhesion and activation.
  • CD2 interacts with its ligand, CD58 (lymphocyte function-associated antigen 3).

Purpose of the Study:

  • To investigate how T-cell receptor-CD3 signaling regulates the CD2-CD58 interaction.
  • To determine the role of CD2 cytoplasmic domain in avidity regulation and T-cell signaling.
  • To assess the impact of CD2 avidity regulation on antigen-specific T-cell responses.

Main Methods:

  • T-cell receptor-CD3 crosslinking using antibodies.
  • Mutational analysis of the CD2 cytoplasmic domain.
  • Assessing CD2 avidity changes upon T-cell receptor stimulation.
  • Evaluating antigen-specific T-cell responses in cell lines.

Main Results:

  • T-cell receptor-CD3 crosslinking rapidly increases CD2 avidity for CD58.
  • A specific asparagine in the CD2 cytoplasmic tail is essential for T-cell receptor-induced avidity changes but not for CD2 signaling.
  • Cell lines with defective CD2 avidity regulation show impaired antigen-specific responses.

Conclusions:

  • CD2-CD58 interaction avidity is dynamically regulated by T-cell receptor-CD3 signaling.
  • The CD2 cytoplasmic domain has distinct functional regions for avidity regulation and signaling.
  • Enhanced CD2 adhesion, through increased avidity, directly contributes to T-cell responsiveness, independent of CD2-mediated signal transduction.

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