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Monoclonal antibody specific for lactosylceramide
The Journal of Biological Chemistry
|May 10, 1984
Summary
The T5A7 antibody specifically targets lactosylceramide, a key molecule on myeloid cells and T-lymphocytes. This finding advances understanding of cell surface antigen recognition and glycolipid specificity.
Area of Science:
- Immunology
- Glycobiology
- Cell Biology
Background:
- The T5A7 hybridoma antibody was initially developed for mapping human myeloid differentiation antigens.
- It recognizes an antigen present on mature myelomonocytic cells and activated T-lymphocytes.
Purpose of the Study:
- To precisely determine the molecular specificity of the T5A7 antibody.
- To investigate the antibody's reactivity with various glycolipids and its potential cross-reactivity.
Main Methods:
- Utilized direct and indirect binding assays with a panel of structurally defined glycolipids.
- Tested antibody reactivity against different lactosylceramide preparations with varying fatty acid compositions.
Main Results:
- The T5A7 antibody specifically binds to lactosylceramide (Gal beta 1----4Glc beta 1----1 Cer).
- No cross-reactivity was observed with N-acetyllactosamine-terminated glycolipids like i and I antigens.
- The study explored the influence of ceramide's fatty acid composition on antibody binding.
Conclusions:
- The T5A7 antibody is a highly specific probe for lactosylceramide.
- This specificity is valuable for research in myeloid cell differentiation and T-lymphocyte subsets.
- Further characterization of ceramide's role in antigen recognition is warranted.