| T cell clones specific for an amphipathic alpha-helical region of sperm whale myoglobin show differing fine specificities for synthetic peptides. A multiview/single structure interpretation of immunodominance. | |
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MedLine Citation:
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PMID: 3490536 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The T cell response to sperm whale myoglobin in the H-2d haplotype has been shown to be largely focused on a limited region around glutamic acid 109 recognized in association with I-Ad. T cell clones 9.27 and 1.2 have been previously (4, 5) shown to reflect this specificity and MHC restriction. In this study we have used a panel of synthetic peptides from the region 102-118 of myoglobin to characterize the specificities of these representative clones. The segment from 106-118 was found to represent a consensus region for recognition by both clones. However, we saw significant differences between clones in the hierarchy of responsiveness to peptides within the panel. In as much as the peptide and the I-Ad molecule remain constant, these differences derive from differences in how each T cell receptor interacts with the antigen. This peptide segment is an amphipathic alpha helix in native myoglobin, meaning that one side is hydrophobic and the other hydrophilic. It is one of the prototype cases that led us to find that amphipathic helices constitute the majority of immunodominant sites recognized by helper T cells (1). It is likely that the peptide will refold into an amphipathic helix stabilized by the interface at the surface of the presenting cell. When such secondary conformation is considered, these data are consistent with a model of multiple T cell specificities arising from multiple views of a single antigen conformation at a single Ia-binding site and do not require postulation of multiple conformations or binding sites. Additionally, the finding of distinct specificities suggests that the immunodominance of this site depends not on the dominance of a single clone, but on the focusing of a polyclonal response on a single region of the molecule in association with I-Ad. The immunodominance of this particular region of the protein may thus depend on intrinsic features of the site, such as potential to form an amphipathic helix, as well as extrinsic factors such as binding properties of the I-A molecule. |
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Authors:
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K B Cease; I Berkower; J York-Jolley; J A Berzofsky |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The Journal of experimental medicine Volume: 164 ISSN: 0022-1007 ISO Abbreviation: J. Exp. Med. Publication Date: 1986 Nov |
Date Detail:
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Created Date: 1986-12-03 Completed Date: 1986-12-03 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2985109R Medline TA: J Exp Med Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 1779-84 Citation Subset: IM |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Binding Sites Clone Cells Histocompatibility Antigens Class II / immunology Mice Myoglobin / analysis, immunology* Peptide Fragments / immunology* Protein Conformation T-Lymphocytes / immunology* Whales |
| Chemical | |
Reg. No./Substance:
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0/Histocompatibility Antigens Class II; 0/Myoglobin; 0/Peptide Fragments |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
| Full Text | |
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Journal Information Journal ID (nlm-ta): J Exp Med ISSN: 0022-1007 ISSN: 1540-9538 Publisher: The Rockefeller University Press |
Article Information Download PDF  Print publication date: Day: 1 Month: 11 Year: 1986 Volume: 164 Issue: 5 First Page: 1779 Last Page: 1784 ID: 2188437 Publisher Id: 87035450 PubMed Id: 3490536 |
| T cell clones specific for an amphipathic alpha-helical region of sperm whale myoglobin show differing fine specificities for synthetic peptides. A multiview/single structure interpretation of immunodominance | |
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