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Presentation of a horse cytochrome c peptide by multiple H-2b class I major histocompatibility complex (MHC) molecules to C57BL/6- and bm1-derived cytotoxic T lymphocytes: presence of a single MHC anchor residue may confer efficient peptide-specific CTL recognition.
Eur J Immunol. 1994 Sep; 24(9):2141-9.EJ

Abstract

In this study the immunogenic tryptic fragment from a horse cytochrome c (cyt c) digest recognized by cytotoxic T lymphocytes (CTL) induced by in vitro peptide stimulation from C57BL/6 (B6) and mutant B6.C-H-2bm1 (bm1) mice is identified. An identical sequence, p40-53, is recognized by CTL from both B6 and bm1 mice. In addition, both B6 bm1 cloned CTL lines display unusual major histocompatibility complex (MHC) class I-restricted recognition of this peptide in that they respond to it in the context of H-2Kb, H-2Db, and H-2Kbm1 class I molecules, although the sequence lacks the usual structural Kb and Db peptide-binding motifs. Truncated analogues which resemble the lengths of naturally processed MHC class I-presented peptides, confer reactivity for B6 and bm1 CTL against EL4 (H-2b) targets as well as the L cell transfectants, L+Kb, L+Db, and L+Kbm1. The antigenic peptide with the greatest potency is p41-49, which appears to be generated by angiotensin converting enzyme cleavage of the full-length p40-53 tryptic peptide. The minimum antigenic peptide recognized by both B6 and bm1 CTL, and which targets lysis on each of the transfectants, is the hexamer p43-48 peptide from horse cyt c. Residues Pro44 and Thr47, which occupy polymorphic positions with respect to other species-variant cyt c molecules, influence recognition of these peptides differently for the B6 and bm1 CTL. The ability of H-2Kb, H-2Db, and mutant H-2Kbm1 class I molecules to present the same peptide to a single cloned CTL is discussed in the context of current knowledge of peptide anchor residues and side chain-specific binding pockets in the MHC class I peptide-binding site.

Authors+Show Affiliations

Department of Microbiology & Immunology, West Virginia University, Morgantown 26506-9177.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7522163

Citation

Sheil, J M., et al. "Presentation of a Horse Cytochrome C Peptide By Multiple H-2b Class I Major Histocompatibility Complex (MHC) Molecules to C57BL/6- and Bm1-derived Cytotoxic T Lymphocytes: Presence of a Single MHC Anchor Residue May Confer Efficient Peptide-specific CTL Recognition." European Journal of Immunology, vol. 24, no. 9, 1994, pp. 2141-9.
Sheil JM, Schell TD, Shepherd SE, et al. Presentation of a horse cytochrome c peptide by multiple H-2b class I major histocompatibility complex (MHC) molecules to C57BL/6- and bm1-derived cytotoxic T lymphocytes: presence of a single MHC anchor residue may confer efficient peptide-specific CTL recognition. Eur J Immunol. 1994;24(9):2141-9.
Sheil, J. M., Schell, T. D., Shepherd, S. E., Klimo, G. F., Kioschos, J. M., & Paterson, Y. (1994). Presentation of a horse cytochrome c peptide by multiple H-2b class I major histocompatibility complex (MHC) molecules to C57BL/6- and bm1-derived cytotoxic T lymphocytes: presence of a single MHC anchor residue may confer efficient peptide-specific CTL recognition. European Journal of Immunology, 24(9), 2141-9.
Sheil JM, et al. Presentation of a Horse Cytochrome C Peptide By Multiple H-2b Class I Major Histocompatibility Complex (MHC) Molecules to C57BL/6- and Bm1-derived Cytotoxic T Lymphocytes: Presence of a Single MHC Anchor Residue May Confer Efficient Peptide-specific CTL Recognition. Eur J Immunol. 1994;24(9):2141-9. PubMed PMID: 7522163.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Presentation of a horse cytochrome c peptide by multiple H-2b class I major histocompatibility complex (MHC) molecules to C57BL/6- and bm1-derived cytotoxic T lymphocytes: presence of a single MHC anchor residue may confer efficient peptide-specific CTL recognition. AU - Sheil,J M, AU - Schell,T D, AU - Shepherd,S E, AU - Klimo,G F, AU - Kioschos,J M, AU - Paterson,Y, PY - 1994/9/1/pubmed PY - 1994/9/1/medline PY - 1994/9/1/entrez SP - 2141 EP - 9 JF - European journal of immunology JO - Eur. J. Immunol. VL - 24 IS - 9 N2 - In this study the immunogenic tryptic fragment from a horse cytochrome c (cyt c) digest recognized by cytotoxic T lymphocytes (CTL) induced by in vitro peptide stimulation from C57BL/6 (B6) and mutant B6.C-H-2bm1 (bm1) mice is identified. An identical sequence, p40-53, is recognized by CTL from both B6 and bm1 mice. In addition, both B6 bm1 cloned CTL lines display unusual major histocompatibility complex (MHC) class I-restricted recognition of this peptide in that they respond to it in the context of H-2Kb, H-2Db, and H-2Kbm1 class I molecules, although the sequence lacks the usual structural Kb and Db peptide-binding motifs. Truncated analogues which resemble the lengths of naturally processed MHC class I-presented peptides, confer reactivity for B6 and bm1 CTL against EL4 (H-2b) targets as well as the L cell transfectants, L+Kb, L+Db, and L+Kbm1. The antigenic peptide with the greatest potency is p41-49, which appears to be generated by angiotensin converting enzyme cleavage of the full-length p40-53 tryptic peptide. The minimum antigenic peptide recognized by both B6 and bm1 CTL, and which targets lysis on each of the transfectants, is the hexamer p43-48 peptide from horse cyt c. Residues Pro44 and Thr47, which occupy polymorphic positions with respect to other species-variant cyt c molecules, influence recognition of these peptides differently for the B6 and bm1 CTL. The ability of H-2Kb, H-2Db, and mutant H-2Kbm1 class I molecules to present the same peptide to a single cloned CTL is discussed in the context of current knowledge of peptide anchor residues and side chain-specific binding pockets in the MHC class I peptide-binding site. SN - 0014-2980 UR - https://www.unboundmedicine.com/medline/citation/7522163/Presentation_of_a_horse_cytochrome_c_peptide_by_multiple_H_2b_class_I_major_histocompatibility_complex__MHC__molecules_to_C57BL/6__and_bm1_derived_cytotoxic_T_lymphocytes:_presence_of_a_single_MHC_anchor_residue_may_confer_efficient_peptide_specific_CTL_recognition_ L2 - https://doi.org/10.1002/eji.1830240931 DB - PRIME DP - Unbound Medicine ER -