Peptide-Independent Folding and CD8αα Binding by the Nonclassical Class I Molecule, Thymic Leukemia Antigen
| Autor: | Jan Pohl, Peter E. Jensen, Dominique A. Weber, Jerrod L. Wigal, Antoine Attinger, Ellis L. Reinherz, Mitchell Kronenberg, Hilde Cheroutre, Yi Xiong, Christopher C. Kemball |
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| Rok vydání: | 2002 |
| Předmět: |
Protein Folding
Circular dichroism Glycosylation CD8 Antigens T-Lymphocytes Immunology Peptide Biosensing Techniques Inclusion bodies law.invention Mice chemistry.chemical_compound Antigen Antigens Neoplasm Peptide Library law HLA-A2 Antigen Animals Humans Immunology and Allergy chemistry.chemical_classification Membrane Glycoproteins Chemistry Beta-2 microglobulin Circular Dichroism Histocompatibility Antigens Class I Mice Inbred C57BL Recombinant DNA Biophysics Thermodynamics Peptides beta 2-Microglobulin Protein Binding Conformational epitope |
| Zdroj: | The Journal of Immunology. 169:5708-5714 |
| ISSN: | 1550-6606 0022-1767 |
| Popis: | The nonclassical class I molecule, thymic leukemia (TL), has been shown to be expressed on intestinal epithelial cells and to interact with CD8+ intraepithelial T lymphocytes. We generated recombinant soluble TL (T18d) H chains in bacteria as inclusion bodies and refolded them with β2-microglobulin in the presence or absence of a random peptide library. Using a mAb, HD168, that recognizes a conformational epitope on native TL molecules, we observed that protein folds efficiently in the absence of peptide. Circular dichroism analysis demonstrated that TL molecules have structural features similar to classical class I molecules. Moreover, thermal denaturation experiments indicated that the melting temperature for peptide-free TL is similar to values reported previously for conventional class I-peptide complexes. Our results also show that CD8αα binding is not dependent on either TL-associated peptide or TL glycosylation. |
| Databáze: | OpenAIRE |
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