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Related Experiment Videos

Mapping the dextran sulfate binding site on CD2.

H S Warren1, C R Parish

  • 1Cancer Research Unit, Woden Valley Hospital, Australia.

Immunology and Cell Biology
|June 1, 1990
PubMed
Summary
This summary is machine-generated.

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Dextran sulfate (DXS) binds to the T11(2) epitope on CD2 molecules on T cells. This interaction suggests that natural ligands for CD2 may involve sulfated carbohydrate structures.

Area of Science:

  • Immunology
  • Molecular Biology
  • Glycobiology

Background:

  • CD2 is a critical adhesion molecule on T lymphocytes involved in immune responses.
  • Understanding CD2 epitope interactions is key to modulating T cell activation.

Purpose of the Study:

  • To identify the binding site of dextran sulfate (DXS) on the CD2 molecule.
  • To investigate the influence of DXS on the binding of anti-CD2 monoclonal antibodies (MoAbs).

Main Methods:

  • Analysis of anti-CD2 monoclonal antibody (MoAb) binding to T cells.
  • Inhibition assays using dextran sulfate (DXS), a sulfated polysaccharide.
  • Characterization of CD2 epitopes T11(1), T11(2), and T11(3).

Main Results:

Related Experiment Videos

  • Dextran sulfate (DXS) primarily binds to the T11(2) epitope of CD2.
  • DXS inhibited the binding of MoAbs targeting the T11(2) epitope.
  • DXS binding augmented the binding of MoAbs targeting the T11(3) epitope, suggesting conformational changes.

    • Conclusions:

    • The T11(2) epitope is the principal binding site for DXS on CD2.
    • CD2-DXS interactions may alter the presentation of other CD2 epitopes.
    • A natural ligand for the T11(2) epitope is likely a sulfated carbohydrate structure.