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[Promiscuous T cell hybridoma derived from NOD mouse]
1Section of Pathology, Hokkaido University, Sapporo, Japan.
[Hokkaido Igaku Zasshi] the Hokkaido Journal of Medical Science
|March 1, 1995
Summary
This study identifies a unique T cell hybridoma, NOE33-1-2, with peculiar characteristics influencing its interaction with antigen-presenting molecules. The findings suggest this hybridoma
Area of Science:
- Immunology
- Molecular Biology
- T cell receptor (TCR) interactions
Context:
- Previous studies defined epitope and agretope sites on the p43-58 peptide of pigeon cytochrome c.
- Specific amino acids at agretopic positions (46 and 54) were identified for binding to I-A or I-E molecules.
- Arginine (R) at position 46 and alanine (A) at position 54 form an agretopic motif for I-Ag7 binding in NOD mice.
Purpose:
- To characterize a promiscuous T cell hybridoma, NOE33-1-2, specific for a p43-58 analogue (46R50E54A).
- To investigate the molecular interactions between the NOE33-1-2 TCR, the 46R50E54A peptide, and MHC class II molecules (I-A and I-Ag7).
- To understand the basis for the unique recognition pattern and high affinity of the NOE33-1-2 hybridoma.
Summary:
- A promiscuous T cell hybridoma, NOE33-1-2, recognized the 46R50E54A analogue across various I-A molecules and I-Ag7.
- The hybridoma's response pattern correlated with peptide-MHC binding affinity but also revealed a profound involvement of the I-Ad beta chain floor in TCR interaction.
- NOE33-1-2 exhibited higher affinity for stimulatory complexes compared to other T cell hybridomas, suggesting unique selection mechanisms.
Impact:
- Reveals a novel TCR-peptide-MHC interaction involving the I-Ad beta chain floor.
- Suggests peculiar selection processes (negative or positive) influencing T cell hybridoma characteristics.
- Provides insights into T cell receptor promiscuity and affinity in the context of specific MHC molecules.