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Structural and functional characterization of the CD2 immunoadhesion domain. Evidence for inclusion of CD2 in an

M A Recny1, E A Neidhardt, P H Sayre

  • 1Laboratory of Immunobiology, Dana-Farber Cancer Institute, Cambridge, Massachusetts.

The Journal of Biological Chemistry
|May 25, 1990
PubMed

Insights

The T-lymphocyte glycoprotein CD2

Area of Science:

  • Immunology
  • Structural Biology
  • Biophysics

Background:

  • T-lymphocyte cell adhesion is crucial for immune responses.
  • CD2 protein mediates T-lymphocyte interactions with other cells via LFA-3 binding.
  • Understanding CD2's structural basis for adhesion is key.

Purpose of the Study:

  • To identify the specific structural components of CD2 responsible for cell adhesion.
  • To analyze the biophysical properties of CD2 domains.

Main Methods:

  • Papain digestion to isolate the amino-terminal domain of CD2.
  • Binding assays to determine LFA-3 interaction affinity (dissociation constant).
  • Monoclonal antibody binding to assess functional epitopes.
  • Circular dichroism spectroscopy to analyze protein secondary structure.

Main Results:

  • The isolated amino-terminal CD2 domain binds LFA-3 with a dissociation constant of 0.4 microM.
  • This domain retains functional immunoadhesion epitopes and inhibits T-cell rosetting.
  • Circular dichroism revealed significant alpha-helical content (22%) in the CD2 adhesion domain.
  • Biophysical data support classification of CD2 within the alpha-beta protein folding class.

Conclusions:

  • All CD2 immunoadhesion functions are localized to its amino-terminal domain.
  • The CD2 adhesion domain exhibits structural characteristics consistent with an alpha-beta protein fold.
  • These findings enhance understanding of T-cell adhesion mechanisms and CD2 structure.

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