Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8+ T cells
Peptide–MHC (pMHC) multimers, in addition to being tools for tracking and quantifying antigen-specific T cells, can mediate downstream signaling after T-cell receptor engagement. In the absence of costimulation, this can lead to anergy or apoptosis of cognate T cells, a property that could be exploi...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2011-08, Vol.108 (33), p.13682-13687 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Samanta, Dibyendu Mukherjee, Gayatri Ramagopal, Udupi A Chaparro, Rodolfo J Nathenson, Stanley G DiLorenzo, Teresa P Almo, Steven C |
| description | Peptide–MHC (pMHC) multimers, in addition to being tools for tracking and quantifying antigen-specific T cells, can mediate downstream signaling after T-cell receptor engagement. In the absence of costimulation, this can lead to anergy or apoptosis of cognate T cells, a property that could be exploited in the setting of autoimmune disease. Most studies with class I pMHC multimers used noncovalently linked peptides, which can allow unwanted CD8+ T-cell activation as a result of peptide transfer to cellular MHC molecules. To circumvent this problem, and given the role of self-reactive CD8+ T cells in the development of type 1 diabetes, we designed a single-chain pMHC complex (scKd.IGRP) by using the class I MHC molecule H-2Kd and a covalently linked peptide derived from islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP206–214), a well established autoantigen in NOD mice. X-ray diffraction studies revealed that the peptide is presented in the groove of the MHC molecule in canonical fashion, and it was also demonstrated that scKd.IGRP tetramers bound specifically to cognate CD8+ T cells. Tetramer binding induced death of naive T cells and in vitro- and in vivo-differentiated cytotoxic T lymphocytes, and tetramer-treated cytotoxic T lymphocytes showed a diminished IFN-γ response to antigen stimulation. Tetramer accessibility to disease-relevant T cells in vivo was also demonstrated. Our study suggests the potential of single-chain pMHC tetramers as possible therapeutic agents in autoimmune disease. Their ability to affect the fate of naive and activated CD8+ T cells makes them a potential intervention strategy in early and late stages of disease. |
| doi_str_mv | 10.1073/pnas.1110971108 |
| format | Article |
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In the absence of costimulation, this can lead to anergy or apoptosis of cognate T cells, a property that could be exploited in the setting of autoimmune disease. Most studies with class I pMHC multimers used noncovalently linked peptides, which can allow unwanted CD8+ T-cell activation as a result of peptide transfer to cellular MHC molecules. To circumvent this problem, and given the role of self-reactive CD8+ T cells in the development of type 1 diabetes, we designed a single-chain pMHC complex (scKd.IGRP) by using the class I MHC molecule H-2Kd and a covalently linked peptide derived from islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP206–214), a well established autoantigen in NOD mice. X-ray diffraction studies revealed that the peptide is presented in the groove of the MHC molecule in canonical fashion, and it was also demonstrated that scKd.IGRP tetramers bound specifically to cognate CD8+ T cells. Tetramer binding induced death of naive T cells and in vitro- and in vivo-differentiated cytotoxic T lymphocytes, and tetramer-treated cytotoxic T lymphocytes showed a diminished IFN-γ response to antigen stimulation. Tetramer accessibility to disease-relevant T cells in vivo was also demonstrated. Our study suggests the potential of single-chain pMHC tetramers as possible therapeutic agents in autoimmune disease. Their ability to affect the fate of naive and activated CD8+ T cells makes them a potential intervention strategy in early and late stages of disease.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1110971108</identifier><identifier>PMID: 21825122</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Anergy ; Animals ; Annexins ; Antigens ; Apoptosis ; Autoantigens ; Autoimmune diseases ; Autoimmune Diseases - drug therapy ; Biological Sciences ; CD8 antigen ; CD8-Positive T-Lymphocytes - drug effects ; CD8-Positive T-Lymphocytes - immunology ; Cell Death - drug effects ; Cytometry ; cytotoxic T-lymphocytes ; Cytotoxicity ; death ; Diabetes mellitus ; Diabetes Mellitus, Type 1 - drug therapy ; Diabetes Mellitus, Type 1 - immunology ; gamma -Interferon ; Glucose-6-phosphatase ; Glucose-6-Phosphatase - immunology ; Histocompatibility antigen H-2 ; Histocompatibility Antigens - chemistry ; Histocompatibility Antigens - pharmacology ; insulin-dependent diabetes mellitus ; interferon-gamma ; Lymphocyte Activation - immunology ; Lymphocytes T ; Major histocompatibility complex ; Mice ; Mice, Inbred NOD ; Mice, Transgenic ; Molecules ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - pharmacology ; Peptides ; Protein Multimerization ; Rodents ; Splenocytes ; Structure-function relationships ; T cell antigen receptors ; T cell receptors ; T lymphocytes ; T-cell receptor ; Type 1 diabetes mellitus ; X-ray diffraction</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2011-08, Vol.108 (33), p.13682-13687</ispartof><rights>copyright © 1993–2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Aug 16, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c555t-2ebfc077714196b4170cbf3c8d9cc2322025ec8a9f7eff78bcfa4c1ac57a1f373</citedby><cites>FETCH-LOGICAL-c555t-2ebfc077714196b4170cbf3c8d9cc2322025ec8a9f7eff78bcfa4c1ac57a1f373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/108/33.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/27979258$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/27979258$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21825122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Samanta, Dibyendu</creatorcontrib><creatorcontrib>Mukherjee, Gayatri</creatorcontrib><creatorcontrib>Ramagopal, Udupi A</creatorcontrib><creatorcontrib>Chaparro, Rodolfo J</creatorcontrib><creatorcontrib>Nathenson, Stanley G</creatorcontrib><creatorcontrib>DiLorenzo, Teresa P</creatorcontrib><creatorcontrib>Almo, Steven C</creatorcontrib><title>Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8+ T cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Peptide–MHC (pMHC) multimers, in addition to being tools for tracking and quantifying antigen-specific T cells, can mediate downstream signaling after T-cell receptor engagement. In the absence of costimulation, this can lead to anergy or apoptosis of cognate T cells, a property that could be exploited in the setting of autoimmune disease. Most studies with class I pMHC multimers used noncovalently linked peptides, which can allow unwanted CD8+ T-cell activation as a result of peptide transfer to cellular MHC molecules. To circumvent this problem, and given the role of self-reactive CD8+ T cells in the development of type 1 diabetes, we designed a single-chain pMHC complex (scKd.IGRP) by using the class I MHC molecule H-2Kd and a covalently linked peptide derived from islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP206–214), a well established autoantigen in NOD mice. X-ray diffraction studies revealed that the peptide is presented in the groove of the MHC molecule in canonical fashion, and it was also demonstrated that scKd.IGRP tetramers bound specifically to cognate CD8+ T cells. Tetramer binding induced death of naive T cells and in vitro- and in vivo-differentiated cytotoxic T lymphocytes, and tetramer-treated cytotoxic T lymphocytes showed a diminished IFN-γ response to antigen stimulation. Tetramer accessibility to disease-relevant T cells in vivo was also demonstrated. Our study suggests the potential of single-chain pMHC tetramers as possible therapeutic agents in autoimmune disease. Their ability to affect the fate of naive and activated CD8+ T cells makes them a potential intervention strategy in early and late stages of disease.</description><subject>Anergy</subject><subject>Animals</subject><subject>Annexins</subject><subject>Antigens</subject><subject>Apoptosis</subject><subject>Autoantigens</subject><subject>Autoimmune diseases</subject><subject>Autoimmune Diseases - drug therapy</subject><subject>Biological Sciences</subject><subject>CD8 antigen</subject><subject>CD8-Positive T-Lymphocytes - drug effects</subject><subject>CD8-Positive T-Lymphocytes - immunology</subject><subject>Cell Death - drug effects</subject><subject>Cytometry</subject><subject>cytotoxic T-lymphocytes</subject><subject>Cytotoxicity</subject><subject>death</subject><subject>Diabetes mellitus</subject><subject>Diabetes Mellitus, Type 1 - drug therapy</subject><subject>Diabetes Mellitus, Type 1 - immunology</subject><subject>gamma -Interferon</subject><subject>Glucose-6-phosphatase</subject><subject>Glucose-6-Phosphatase - immunology</subject><subject>Histocompatibility antigen H-2</subject><subject>Histocompatibility Antigens - chemistry</subject><subject>Histocompatibility Antigens - pharmacology</subject><subject>insulin-dependent diabetes mellitus</subject><subject>interferon-gamma</subject><subject>Lymphocyte Activation - immunology</subject><subject>Lymphocytes T</subject><subject>Major histocompatibility complex</subject><subject>Mice</subject><subject>Mice, Inbred NOD</subject><subject>Mice, Transgenic</subject><subject>Molecules</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - pharmacology</subject><subject>Peptides</subject><subject>Protein Multimerization</subject><subject>Rodents</subject><subject>Splenocytes</subject><subject>Structure-function relationships</subject><subject>T cell antigen receptors</subject><subject>T cell receptors</subject><subject>T lymphocytes</subject><subject>T-cell receptor</subject><subject>Type 1 diabetes mellitus</subject><subject>X-ray diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk1v1DAQhiMEokvhzAmwuICE0vojju0LElo-ilTEoe3Zchx716tsnNrOSnDiyJ1_yC_BIUsXOMDF9nieecfjmaJ4iOAJgoycDr2KJwghKFhe-K1ikY-orCsBbxcLCDEreYWro-JejBsIoaAc3i2OMOKYIowXxdeLFEadxqA6oPoW2LHXyfk-m3qtgtLJBPdZTVfAW6BAdP2qM2V2uh4MZkiuNd-_fPtwtgRb3xk9dgaktUrZasdOJRNB49Ma9MrtzM8UWdPtsqMFy9f8BbgE2nRdvF_csaqL5sF-Py6u3r65XJ6V5x_fvV--Oi81pTSV2DRWQ8YYqpComwoxqBtLNG-F1phgDDE1mithmbGW8UZbVWmkNGUKWcLIcfFy1h3GZmtabfqUa5dDcFsVPkmvnPzT07u1XPmdJIhyJCaBZ3uB4K9HE5PcujiVoHrjxygFZPlRvEL_JXluTS1qRjP5_J8kqmtCK47ohD79C934MeR-zXpC0Jpn6HSGdPAxBmNv6kNQToMjp8GRh8HJEY9__5Yb_tekZADsgSnyIMclIRKRmk_IoxnZxOTDQYIJJjCdcjyZ_VZ5qVbBRXl1gSGqIMxZBKzID7z93uU</recordid><startdate>20110816</startdate><enddate>20110816</enddate><creator>Samanta, Dibyendu</creator><creator>Mukherjee, Gayatri</creator><creator>Ramagopal, Udupi A</creator><creator>Chaparro, Rodolfo J</creator><creator>Nathenson, Stanley G</creator><creator>DiLorenzo, Teresa P</creator><creator>Almo, Steven C</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110816</creationdate><title>Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8+ T cells</title><author>Samanta, Dibyendu ; Mukherjee, Gayatri ; Ramagopal, Udupi A ; Chaparro, Rodolfo J ; Nathenson, Stanley G ; DiLorenzo, Teresa P ; Almo, Steven C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c555t-2ebfc077714196b4170cbf3c8d9cc2322025ec8a9f7eff78bcfa4c1ac57a1f373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Anergy</topic><topic>Animals</topic><topic>Annexins</topic><topic>Antigens</topic><topic>Apoptosis</topic><topic>Autoantigens</topic><topic>Autoimmune diseases</topic><topic>Autoimmune Diseases - drug therapy</topic><topic>Biological Sciences</topic><topic>CD8 antigen</topic><topic>CD8-Positive T-Lymphocytes - drug effects</topic><topic>CD8-Positive T-Lymphocytes - immunology</topic><topic>Cell Death - drug effects</topic><topic>Cytometry</topic><topic>cytotoxic T-lymphocytes</topic><topic>Cytotoxicity</topic><topic>death</topic><topic>Diabetes mellitus</topic><topic>Diabetes Mellitus, Type 1 - drug therapy</topic><topic>Diabetes Mellitus, Type 1 - immunology</topic><topic>gamma -Interferon</topic><topic>Glucose-6-phosphatase</topic><topic>Glucose-6-Phosphatase - immunology</topic><topic>Histocompatibility antigen H-2</topic><topic>Histocompatibility Antigens - chemistry</topic><topic>Histocompatibility Antigens - pharmacology</topic><topic>insulin-dependent diabetes mellitus</topic><topic>interferon-gamma</topic><topic>Lymphocyte Activation - immunology</topic><topic>Lymphocytes T</topic><topic>Major histocompatibility complex</topic><topic>Mice</topic><topic>Mice, Inbred NOD</topic><topic>Mice, Transgenic</topic><topic>Molecules</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - pharmacology</topic><topic>Peptides</topic><topic>Protein Multimerization</topic><topic>Rodents</topic><topic>Splenocytes</topic><topic>Structure-function relationships</topic><topic>T cell antigen receptors</topic><topic>T cell receptors</topic><topic>T lymphocytes</topic><topic>T-cell receptor</topic><topic>Type 1 diabetes mellitus</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Samanta, Dibyendu</creatorcontrib><creatorcontrib>Mukherjee, Gayatri</creatorcontrib><creatorcontrib>Ramagopal, Udupi A</creatorcontrib><creatorcontrib>Chaparro, Rodolfo J</creatorcontrib><creatorcontrib>Nathenson, Stanley G</creatorcontrib><creatorcontrib>DiLorenzo, Teresa P</creatorcontrib><creatorcontrib>Almo, Steven C</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Samanta, Dibyendu</au><au>Mukherjee, Gayatri</au><au>Ramagopal, Udupi A</au><au>Chaparro, Rodolfo J</au><au>Nathenson, Stanley G</au><au>DiLorenzo, Teresa P</au><au>Almo, Steven C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8+ T cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2011-08-16</date><risdate>2011</risdate><volume>108</volume><issue>33</issue><spage>13682</spage><epage>13687</epage><pages>13682-13687</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Peptide–MHC (pMHC) multimers, in addition to being tools for tracking and quantifying antigen-specific T cells, can mediate downstream signaling after T-cell receptor engagement. In the absence of costimulation, this can lead to anergy or apoptosis of cognate T cells, a property that could be exploited in the setting of autoimmune disease. Most studies with class I pMHC multimers used noncovalently linked peptides, which can allow unwanted CD8+ T-cell activation as a result of peptide transfer to cellular MHC molecules. To circumvent this problem, and given the role of self-reactive CD8+ T cells in the development of type 1 diabetes, we designed a single-chain pMHC complex (scKd.IGRP) by using the class I MHC molecule H-2Kd and a covalently linked peptide derived from islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP206–214), a well established autoantigen in NOD mice. X-ray diffraction studies revealed that the peptide is presented in the groove of the MHC molecule in canonical fashion, and it was also demonstrated that scKd.IGRP tetramers bound specifically to cognate CD8+ T cells. Tetramer binding induced death of naive T cells and in vitro- and in vivo-differentiated cytotoxic T lymphocytes, and tetramer-treated cytotoxic T lymphocytes showed a diminished IFN-γ response to antigen stimulation. Tetramer accessibility to disease-relevant T cells in vivo was also demonstrated. Our study suggests the potential of single-chain pMHC tetramers as possible therapeutic agents in autoimmune disease. Their ability to affect the fate of naive and activated CD8+ T cells makes them a potential intervention strategy in early and late stages of disease.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>21825122</pmid><doi>10.1073/pnas.1110971108</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2011-08, Vol.108 (33), p.13682-13687 |
| issn | 0027-8424 1091-6490 |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Anergy Animals Annexins Antigens Apoptosis Autoantigens Autoimmune diseases Autoimmune Diseases - drug therapy Biological Sciences CD8 antigen CD8-Positive T-Lymphocytes - drug effects CD8-Positive T-Lymphocytes - immunology Cell Death - drug effects Cytometry cytotoxic T-lymphocytes Cytotoxicity death Diabetes mellitus Diabetes Mellitus, Type 1 - drug therapy Diabetes Mellitus, Type 1 - immunology gamma -Interferon Glucose-6-phosphatase Glucose-6-Phosphatase - immunology Histocompatibility antigen H-2 Histocompatibility Antigens - chemistry Histocompatibility Antigens - pharmacology insulin-dependent diabetes mellitus interferon-gamma Lymphocyte Activation - immunology Lymphocytes T Major histocompatibility complex Mice Mice, Inbred NOD Mice, Transgenic Molecules Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - pharmacology Peptides Protein Multimerization Rodents Splenocytes Structure-function relationships T cell antigen receptors T cell receptors T lymphocytes T-cell receptor Type 1 diabetes mellitus X-ray diffraction |
| title | Structural and functional characterization of a single-chain peptide–MHC molecule that modulates both naive and activated CD8+ T cells |
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