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Related Experiment Videos

Class I MHC alpha 3 domain can function as an independent structural unit to bind CD8 alpha

J Fayen1, J H Huang, H Meyerson

  • 1Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA.

Molecular Immunology
|March 1, 1995
PubMed
Summary

This study reveals that CD8 alpha directly binds to the alpha 3 domain of class I MHC molecules. This interaction is specific and does not require other cellular components for T cell recognition.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Cytotoxic T cell function relies on CD8-mediated interactions with target cells.
  • CD8 interacts with a specific region on the alpha 3 domain of class I MHC molecules.

Purpose of the Study:

  • To develop a cell-free assay to directly measure the molecular interaction between CD8 and class I MHC.
  • To characterize the binding kinetics and specificity of this interaction.

Main Methods:

  • A cell-free system using soluble CD8 alpha and a plate-bound HLA-A2.1 alpha 3/MalE fusion protein.
  • Measurement of binding affinity (Kd) and inhibition studies using monoclonal antibodies.

Main Results:

  • Demonstrated specific and saturable binding between soluble CD8 alpha and the alpha 3 domain.

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  • Determined the dissociation constant (Kd) for this interaction to be 4.5 x 10(-7) M.
  • Monoclonal antibodies targeting CD8 or the alpha 3 domain inhibited binding, while others did not.

    • Conclusions:

    • The interaction between CD8 alpha and the class I MHC alpha 3 domain is direct and specific.
    • This interaction does not necessitate neighboring class I MHC sequences or beta 2-microglobulin.