A novel single chain I-A(b) molecule can stimulate and stain antigen-specific T cells
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 uniqu...
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Veröffentlicht in: | Molecular immunology 2003-05, Vol.39 (14), p.861-870 |
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creator | Thayer, Wesley P Dao, Chinh T Ignatowicz, Leszek Jensen, Peter E |
description | 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 Ealpha 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. |
doi_str_mv | 10.1016/S0161-5890(03)00010-5 |
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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 Ealpha 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.</description><identifier>ISSN: 0161-5890</identifier><identifier>DOI: 10.1016/S0161-5890(03)00010-5</identifier><identifier>PMID: 12686502</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, Differentiation, B-Lymphocyte - genetics ; Base Sequence ; Cell Line ; Cell Membrane - immunology ; Cercopithecus aethiops ; COS Cells ; Genes, MHC Class II ; Genes, Synthetic ; Histocompatibility Antigens Class II - genetics ; Histocompatibility Antigens Class II - immunology ; Humans ; Immunoglobulin G - genetics ; Immunoglobulin G - immunology ; Isoantibodies - immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nucleopolyhedrovirus - genetics ; Recombinant Fusion Proteins - immunology ; Repetitive Sequences, Amino Acid ; Solubility ; Spodoptera - cytology ; Structure-Activity Relationship ; T-Lymphocyte Subsets - immunology ; Transfection</subject><ispartof>Molecular immunology, 2003-05, Vol.39 (14), p.861-870</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12686502$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thayer, Wesley P</creatorcontrib><creatorcontrib>Dao, Chinh T</creatorcontrib><creatorcontrib>Ignatowicz, Leszek</creatorcontrib><creatorcontrib>Jensen, Peter E</creatorcontrib><title>A novel single chain I-A(b) molecule can stimulate and stain antigen-specific T cells</title><title>Molecular immunology</title><addtitle>Mol Immunol</addtitle><description>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 Ealpha 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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Differentiation, B-Lymphocyte - genetics</subject><subject>Base Sequence</subject><subject>Cell Line</subject><subject>Cell Membrane - immunology</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Genes, MHC Class II</subject><subject>Genes, Synthetic</subject><subject>Histocompatibility Antigens Class II - genetics</subject><subject>Histocompatibility Antigens Class II - immunology</subject><subject>Humans</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin G - immunology</subject><subject>Isoantibodies - immunology</subject><subject>Lymphocyte Activation</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Molecular Sequence Data</subject><subject>Nucleopolyhedrovirus - genetics</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Repetitive Sequences, Amino Acid</subject><subject>Solubility</subject><subject>Spodoptera - cytology</subject><subject>Structure-Activity Relationship</subject><subject>T-Lymphocyte Subsets - immunology</subject><subject>Transfection</subject><issn>0161-5890</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPwzAQhH0A0VL4CSCfUHsweO3YsY9VxaNSJQ6058ixnWKUOKFOkPj3pOJx5bKjnf00Gi1CV0BvgYK8exkHEKE0nVO-oJQCJeIETf_sCTpP6W08SCrFGZoAk0oKyqZot8Sx_fA1TiHua4_tqwkRr8lyXi5w09beDkfXRJz60Ay16T020Y3bkTOxD3sfSeq8DVWweIutr-t0gU4rUyd_-aMztHu4366eyOb5cb1abkjHuOpJpkELVzqnQEtfWSm1gtxTyBilIi8NCKYddWNdXrEShOLC8ryypdJM6pzP0M13bndo3wef-qIJ6djARN8Oqcg5SAVK_AuCylmmMjaC1z_gUDbeFd0hNObwWfx-jH8BQLVp3w</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Thayer, Wesley P</creator><creator>Dao, Chinh T</creator><creator>Ignatowicz, Leszek</creator><creator>Jensen, Peter E</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20030501</creationdate><title>A novel single chain I-A(b) molecule can stimulate and stain antigen-specific T cells</title><author>Thayer, Wesley P ; Dao, Chinh T ; Ignatowicz, Leszek ; Jensen, Peter E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p238t-49195dbdd8196efc669817e01420057ba1529d0d1263f2b15835c37fcb8926973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Differentiation, B-Lymphocyte - genetics</topic><topic>Base Sequence</topic><topic>Cell Line</topic><topic>Cell Membrane - immunology</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Genes, MHC Class II</topic><topic>Genes, Synthetic</topic><topic>Histocompatibility Antigens Class II - genetics</topic><topic>Histocompatibility Antigens Class II - immunology</topic><topic>Humans</topic><topic>Immunoglobulin G - genetics</topic><topic>Immunoglobulin G - immunology</topic><topic>Isoantibodies - immunology</topic><topic>Lymphocyte Activation</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Molecular Sequence Data</topic><topic>Nucleopolyhedrovirus - genetics</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Repetitive Sequences, Amino Acid</topic><topic>Solubility</topic><topic>Spodoptera - cytology</topic><topic>Structure-Activity Relationship</topic><topic>T-Lymphocyte Subsets - immunology</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thayer, Wesley P</creatorcontrib><creatorcontrib>Dao, Chinh T</creatorcontrib><creatorcontrib>Ignatowicz, Leszek</creatorcontrib><creatorcontrib>Jensen, Peter E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thayer, Wesley P</au><au>Dao, Chinh T</au><au>Ignatowicz, Leszek</au><au>Jensen, Peter E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel single chain I-A(b) molecule can stimulate and stain antigen-specific T cells</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>39</volume><issue>14</issue><spage>861</spage><epage>870</epage><pages>861-870</pages><issn>0161-5890</issn><abstract>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 Ealpha 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.</abstract><cop>England</cop><pmid>12686502</pmid><doi>10.1016/S0161-5890(03)00010-5</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Antigens, Differentiation, B-Lymphocyte - genetics Base Sequence Cell Line Cell Membrane - immunology Cercopithecus aethiops COS Cells Genes, MHC Class II Genes, Synthetic Histocompatibility Antigens Class II - genetics Histocompatibility Antigens Class II - immunology Humans Immunoglobulin G - genetics Immunoglobulin G - immunology Isoantibodies - immunology Lymphocyte Activation Mice Mice, Inbred C57BL Molecular Sequence Data Nucleopolyhedrovirus - genetics Recombinant Fusion Proteins - immunology Repetitive Sequences, Amino Acid Solubility Spodoptera - cytology Structure-Activity Relationship T-Lymphocyte Subsets - immunology Transfection |
title | A novel single chain I-A(b) molecule can stimulate and stain antigen-specific T cells |
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