A novel single chain I-Ab molecule can stimulate and stain antigen-specific T cells
| Autor: | Wesley P. Thayer, Leszek Ignatowicz, Peter E. Jensen, Chinh T. Dao |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Repetitive Sequences
Amino Acid CD74 Stereochemistry Recombinant Fusion Proteins T cell Genes MHC Class II Molecular Sequence Data Immunology Antigen presentation Peptide binding Spodoptera Lymphocyte Activation Transfection Major histocompatibility complex Cell Line Mice Structure-Activity Relationship Isoantibodies T-Lymphocyte Subsets Chlorocebus aethiops MHC class I Genes Synthetic medicine Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence Base Sequence biology Chemistry Cell Membrane Histocompatibility Antigens Class II MHC restriction Molecular biology Nucleopolyhedroviruses Antigens Differentiation B-Lymphocyte Mice Inbred C57BL medicine.anatomical_structure Solubility Immunoglobulin G COS Cells biology.protein |
| Zdroj: | Molecular Immunology. 39:861-870 |
| ISSN: | 0161-5890 |
| Popis: | Multimers of soluble major histocompatibility complex class I and II molecules have proven to be useful reagents in quantifying and following specific T cell populations. This study describes the design, generation, and characterization of a novel, single chain I-A b molecule which utilizes a unique linker derived from the murine invariant chain. A fragment of the invariant chain, residues 58–85, binds to a region proximal to the class II peptide binding groove and stabilizes occupancy of the class II invariant chain-associated peptide. We have utilized this fragment, replacing CLIP with the Eα peptide sequence, to lock the attached peptide into the class II binding groove. The single chain I-A b molecule was recognized by a panel of conformation-sensitive, I-A b -specific, monoclonal antibodies. Membrane-bound and soluble forms of the single chain I-A b stimulated an antigen-specific T cell hybridoma, and tetramers made from soluble monomers stained these cells. The unique features of this molecule may be useful in the design of recombinant T cell receptor ligands containing peptides with low affinity for MHC. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect