T lymphocyte response to bacteriophage lambda repressor cI protein. Recognition of the same peptide presented by Ia molecules of different haplotypes
- PMID: 2961803
T lymphocyte response to bacteriophage lambda repressor cI protein. Recognition of the same peptide presented by Ia molecules of different haplotypes
Abstract
The murine T cell response to bacteriophage lambda cI repressor protein has been investigated. Isolation and characterization of class II-restricted T cell hybridomas from BALB/c and A/J mice undergoing a primary response has revealed that a single region of the protein, residues 12-26, is the immunodominant site. Fine specificity analysis using truncated peptides (P12-24 and P15-26) reveals a great deal of heterogeneity at the clonal level of I-Ad-restricted T cells. I-Ek-restricted T cells are less heterogeneous in their reactivity toward P12-24 and P15-26, but show diversity in their responses to peptide analogues with substitution at Tyr22. The specificity difference between T cell hybridomas of I-Ad-restriction and I-Ek-restriction and the inhibition effect of different inactive peptides suggest that the same peptide is presented in different configurations by different Ia molecules. Further, no cross-reactivity can be detected between T cells of these two haplotypes, Ia molecules and Ia bound-peptides.
Similar articles
-
T cell receptor gene usage in the response to lambda repressor cI protein. An apparent bias in the usage of a V alpha gene element.J Exp Med. 1988 Sep 1;168(3):1081-97. doi: 10.1084/jem.168.3.1081. J Exp Med. 1988. PMID: 2971753 Free PMC article.
-
Restricted V-(D)-J junctional regions in the T cell response to lambda-repressor. Identification of residues critical for antigen recognition.J Immunol. 1990 Jun 15;144(12):4851-6. J Immunol. 1990. PMID: 1693642
-
T cell epitope selection: dominance may be determined by both affinity for major histocompatibility complex and stoichiometry of epitope.Eur J Immunol. 1992 Apr;22(4):943-9. doi: 10.1002/eji.1830220410. Eur J Immunol. 1992. PMID: 1372561
-
Immunological activity of covalently linked T-cell epitopes.Nature. 1990 Jan 25;343(6256):381-3. doi: 10.1038/343381a0. Nature. 1990. PMID: 1689012
-
Interaction of peptide antigens and class II major histocompatibility complex antigens.Nature. 1986 Nov 20-26;324(6094):260-2. doi: 10.1038/324260a0. Nature. 1986. PMID: 2946957
Cited by
-
T cell receptor gene usage in the response to lambda repressor cI protein. An apparent bias in the usage of a V alpha gene element.J Exp Med. 1988 Sep 1;168(3):1081-97. doi: 10.1084/jem.168.3.1081. J Exp Med. 1988. PMID: 2971753 Free PMC article.
-
T cell receptor interaction with peptide/major histocompatibility complex (MHC) and superantigen/MHC ligands is dominated by antigen.J Exp Med. 1993 Aug 1;178(2):713-22. doi: 10.1084/jem.178.2.713. J Exp Med. 1993. PMID: 8393480 Free PMC article.
-
Genetically transferred central and peripheral immune tolerance via retroviral-mediated expression of immunogenic epitopes in hematopoietic progenitors or peripheral B lymphocytes.Mol Med. 1997 Mar;3(3):212-24. Mol Med. 1997. PMID: 9100227 Free PMC article.
-
Analysis of peptide binding patterns in different major histocompatibility complex/T cell receptor complexes using pigeon cytochrome c-specific T cell hybridomas. Evidence that a single peptide binds major histocompatibility complex in different conformations.J Exp Med. 1989 Nov 1;170(5):1609-25. doi: 10.1084/jem.170.5.1609. J Exp Med. 1989. PMID: 2553848 Free PMC article.
-
Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH.J Exp Med. 1991 Jul 1;174(1):219-28. doi: 10.1084/jem.174.1.219. J Exp Med. 1991. PMID: 1829108 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Other Literature Sources
Research Materials