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Updated: Aug 10, 2026
09:14
Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Structural and functional epitopes of the human adhesion receptor CD58 (LFA-3)
T J Dengler1, J C Hoffmann, P Knolle
1Division of Applied Immunology, German Cancer Research Center, Heidelberg.
European Journal of Immunology
|November 1, 1992
Summary
Researchers characterized novel epitopes on CD58 (lymphocyte function-associated antigen 3), a key molecule in T cell activation. This work provides new tools for studying CD58 interactions and T cell responses.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- CD58 (lymphocyte function-associated antigen 3) is a crucial cell surface protein involved in T cell adhesion and activation.
- While the CD2 receptor's epitopes are well-defined, detailed functional characterization of CD58 epitopes is lacking.
Purpose of the Study:
- To identify and functionally characterize novel epitopes on the human CD58 molecule.
- To develop new monoclonal antibodies for detecting CD58 and its interactions.
Main Methods:
- Generation of a panel of murine monoclonal antibodies against recombinant human CD58.
- Epitope mapping and functional assays to assess CD58-CD2 interactions and T cell activation.
- Detection of CD58 in serum and on blood cells using newly developed antibodies.
Main Results:
- Six structurally and/or functionally distinct CD58 epitopes were identified.
- Two epitopes are functionally relevant for CD58-CD2 binding and T cell activation.
- New monoclonal antibodies enable detection of CD58 bound to CD2 in biological samples.
Conclusions:
- The study provides a comprehensive characterization of CD58 epitopes, revealing functionally important sites.
- Novel monoclonal antibodies offer improved tools for immunological research and diagnostics involving CD58 and T cell activation.
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