Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen
The T‐cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high‐avidity T‐cell clones recognize the immunodominant pp65 peptide antigen pp65495–5...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2009-11, Vol.65 (11), p.1157-1161 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Reiser, Jean-Baptiste Legoux, François Machillot, Paul Debeaupuis, Emilie Le Moullac-Vaydie, Béatrice Chouquet, Anne Saulquin, Xavier Bonneville, Marc Housset, Dominique |
| description | The T‐cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high‐avidity T‐cell clones recognize the immunodominant pp65 peptide antigen pp65495–503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA‐A2 in a similar manner, several public high‐affinity T‐cell receptors (TCRs) specific for the pp65495–503–HLA‐A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7 Å resolution for the RA15 TCR in complex with the pp65495–503–HLA‐A2 complex. Comparison of the RA15–pp65495–503–HLA‐A2 complex molecular‐replacement solution with the structure of another high‐affinity pp65495–503–HLA‐A2‐specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide‐readout mode. However, the position of the RA15 Vβ domain is significantly shifted, suggesting a different interatomic interaction network. |
| doi_str_mv | 10.1107/S1744309109037890 |
| format | Article |
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In order to check whether all the selected high‐avidity T‐cell clones recognize the immunodominant pp65 peptide antigen pp65495–503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA‐A2 in a similar manner, several public high‐affinity T‐cell receptors (TCRs) specific for the pp65495–503–HLA‐A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7 Å resolution for the RA15 TCR in complex with the pp65495–503–HLA‐A2 complex. Comparison of the RA15–pp65495–503–HLA‐A2 complex molecular‐replacement solution with the structure of another high‐affinity pp65495–503–HLA‐A2‐specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide‐readout mode. However, the position of the RA15 Vβ domain is significantly shifted, suggesting a different interatomic interaction network.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S1744309109037890</identifier><identifier>PMID: 19923740</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>affinity ; Antigens, Viral - chemistry ; Antigens, Viral - genetics ; Antigens, Viral - immunology ; Crystallization ; Crystallization Communications ; Crystallography, X-Ray ; Cytomegalovirus - chemistry ; Cytomegalovirus - immunology ; HLA-A2 ; HLA-A2 Antigen - chemistry ; HLA-A2 Antigen - genetics ; HLA-A2 Antigen - immunology ; human cytomegalovirus ; Humans ; Immunodominant Epitopes - chemistry ; Immunodominant Epitopes - genetics ; Immunodominant Epitopes - immunology ; Models, Molecular ; Molecular Sequence Data ; Peptides - chemistry ; Peptides - genetics ; Peptides - immunology ; Protein Conformation ; public response ; Receptors, Antigen, T-Cell - chemistry ; Receptors, Antigen, T-Cell - immunology ; selection ; T-cell receptors ; X-Ray Diffraction</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2009-11, Vol.65 (11), p.1157-1161</ispartof><rights>International Union of Crystallography, 2009</rights><rights>International Union of Crystallography 2009 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4863-2773c6233cd7b073a7f8a9b88b1e2943a3d7a94d946e7866b524c3ffbf3d9f2f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777048/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777048/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,27901,27902,45550,45551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19923740$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reiser, Jean-Baptiste</creatorcontrib><creatorcontrib>Legoux, François</creatorcontrib><creatorcontrib>Machillot, Paul</creatorcontrib><creatorcontrib>Debeaupuis, Emilie</creatorcontrib><creatorcontrib>Le Moullac-Vaydie, Béatrice</creatorcontrib><creatorcontrib>Chouquet, Anne</creatorcontrib><creatorcontrib>Saulquin, Xavier</creatorcontrib><creatorcontrib>Bonneville, Marc</creatorcontrib><creatorcontrib>Housset, Dominique</creatorcontrib><title>Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>The T‐cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high‐avidity T‐cell clones recognize the immunodominant pp65 peptide antigen pp65495–503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA‐A2 in a similar manner, several public high‐affinity T‐cell receptors (TCRs) specific for the pp65495–503–HLA‐A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7 Å resolution for the RA15 TCR in complex with the pp65495–503–HLA‐A2 complex. Comparison of the RA15–pp65495–503–HLA‐A2 complex molecular‐replacement solution with the structure of another high‐affinity pp65495–503–HLA‐A2‐specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide‐readout mode. However, the position of the RA15 Vβ domain is significantly shifted, suggesting a different interatomic interaction network.</description><subject>affinity</subject><subject>Antigens, Viral - chemistry</subject><subject>Antigens, Viral - genetics</subject><subject>Antigens, Viral - immunology</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>Cytomegalovirus - chemistry</subject><subject>Cytomegalovirus - immunology</subject><subject>HLA-A2</subject><subject>HLA-A2 Antigen - chemistry</subject><subject>HLA-A2 Antigen - genetics</subject><subject>HLA-A2 Antigen - immunology</subject><subject>human cytomegalovirus</subject><subject>Humans</subject><subject>Immunodominant Epitopes - chemistry</subject><subject>Immunodominant Epitopes - genetics</subject><subject>Immunodominant Epitopes - immunology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - immunology</subject><subject>Protein Conformation</subject><subject>public response</subject><subject>Receptors, Antigen, T-Cell - chemistry</subject><subject>Receptors, Antigen, T-Cell - immunology</subject><subject>selection</subject><subject>T-cell receptors</subject><subject>X-Ray Diffraction</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUd1uFCEUJsbG1tUH8MZw59UoDOww3JjUSVs1rUatWq_IGQZ2UeZHYG3XJ_Cxy2bXWuOF3MA55_s55EPoESVPKSXi2QcqOGdEUiIJE7Ukd9DBplVsendvvffR_Ri_EsKYrOp7aJ9KWTLByQH61YR1TOC9-wnJjQOGocNTMN71boCwxhdFgDXWO9S4CDAtncZ6CQF0MuE3b7QY8LRqfR42Z5-KOBntbC7Om_fYDViP_eTNFb50aYldirmxGCCZbJjcwgwP0J4FH83D3T1DH4-PzpuXxenbk1fN4WmheV2xohSC6apkTHeiJYKBsDXItq5bakrJGbBOgOSd5JURdVW185JrZm1rWSdtadkMPd_q5l1702kzpABeTcH1-btqBKf-ngxuqRbjD5WdBeF1FniyEwjj95WJSfUuauM9DGZcRSUYp1zmk5F0i9RhjDEYe-NCidoEqP4JMHMe317vD2OXWAbILeDSebP-v6I6_HJcXryYb8KfoWLLdTGZqxsuhG-qEkzM1ec3J-ode302J1mvZteJz7jy</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Reiser, Jean-Baptiste</creator><creator>Legoux, François</creator><creator>Machillot, Paul</creator><creator>Debeaupuis, Emilie</creator><creator>Le Moullac-Vaydie, Béatrice</creator><creator>Chouquet, Anne</creator><creator>Saulquin, Xavier</creator><creator>Bonneville, Marc</creator><creator>Housset, Dominique</creator><general>International Union of Crystallography</general><scope>BSCLL</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>200911</creationdate><title>Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen</title><author>Reiser, Jean-Baptiste ; Legoux, François ; Machillot, Paul ; Debeaupuis, Emilie ; Le Moullac-Vaydie, Béatrice ; Chouquet, Anne ; Saulquin, Xavier ; Bonneville, Marc ; Housset, Dominique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4863-2773c6233cd7b073a7f8a9b88b1e2943a3d7a94d946e7866b524c3ffbf3d9f2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>affinity</topic><topic>Antigens, Viral - chemistry</topic><topic>Antigens, Viral - genetics</topic><topic>Antigens, Viral - immunology</topic><topic>Crystallization</topic><topic>Crystallization Communications</topic><topic>Crystallography, X-Ray</topic><topic>Cytomegalovirus - chemistry</topic><topic>Cytomegalovirus - immunology</topic><topic>HLA-A2</topic><topic>HLA-A2 Antigen - chemistry</topic><topic>HLA-A2 Antigen - genetics</topic><topic>HLA-A2 Antigen - immunology</topic><topic>human cytomegalovirus</topic><topic>Humans</topic><topic>Immunodominant Epitopes - chemistry</topic><topic>Immunodominant Epitopes - genetics</topic><topic>Immunodominant Epitopes - immunology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - immunology</topic><topic>Protein Conformation</topic><topic>public response</topic><topic>Receptors, Antigen, T-Cell - chemistry</topic><topic>Receptors, Antigen, T-Cell - immunology</topic><topic>selection</topic><topic>T-cell receptors</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reiser, Jean-Baptiste</creatorcontrib><creatorcontrib>Legoux, François</creatorcontrib><creatorcontrib>Machillot, Paul</creatorcontrib><creatorcontrib>Debeaupuis, Emilie</creatorcontrib><creatorcontrib>Le Moullac-Vaydie, Béatrice</creatorcontrib><creatorcontrib>Chouquet, Anne</creatorcontrib><creatorcontrib>Saulquin, Xavier</creatorcontrib><creatorcontrib>Bonneville, Marc</creatorcontrib><creatorcontrib>Housset, Dominique</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reiser, Jean-Baptiste</au><au>Legoux, François</au><au>Machillot, Paul</au><au>Debeaupuis, Emilie</au><au>Le Moullac-Vaydie, Béatrice</au><au>Chouquet, Anne</au><au>Saulquin, Xavier</au><au>Bonneville, Marc</au><au>Housset, Dominique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2009-11</date><risdate>2009</risdate><volume>65</volume><issue>11</issue><spage>1157</spage><epage>1161</epage><pages>1157-1161</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>The T‐cell response to human cytomegalovirus is characterized by a dramatic reduction of clonal diversity in patients undergoing chronic inflammation or immunodepression. In order to check whether all the selected high‐avidity T‐cell clones recognize the immunodominant pp65 peptide antigen pp65495–503 (NLVPMVATV) presented by the major histocompatibility complex (MHC) molecule HLA‐A2 in a similar manner, several public high‐affinity T‐cell receptors (TCRs) specific for the pp65495–503–HLA‐A2 complex have been investigated. Expression, purification and crystallization were performed and preliminary crystallographic data were collected to 4.7 Å resolution for the RA15 TCR in complex with the pp65495–503–HLA‐A2 complex. Comparison of the RA15–pp65495–503–HLA‐A2 complex molecular‐replacement solution with the structure of another high‐affinity pp65495–503–HLA‐A2‐specific TCR, RA14, shows a shared docking mode, indicating that the clonal focusing could be accompanied by the selection of a most favoured peptide‐readout mode. However, the position of the RA15 Vβ domain is significantly shifted, suggesting a different interatomic interaction network.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>19923740</pmid><doi>10.1107/S1744309109037890</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | affinity Antigens, Viral - chemistry Antigens, Viral - genetics Antigens, Viral - immunology Crystallization Crystallization Communications Crystallography, X-Ray Cytomegalovirus - chemistry Cytomegalovirus - immunology HLA-A2 HLA-A2 Antigen - chemistry HLA-A2 Antigen - genetics HLA-A2 Antigen - immunology human cytomegalovirus Humans Immunodominant Epitopes - chemistry Immunodominant Epitopes - genetics Immunodominant Epitopes - immunology Models, Molecular Molecular Sequence Data Peptides - chemistry Peptides - genetics Peptides - immunology Protein Conformation public response Receptors, Antigen, T-Cell - chemistry Receptors, Antigen, T-Cell - immunology selection T-cell receptors X-Ray Diffraction |
| title | Crystallization and preliminary X-ray crystallographic characterization of a public CMV-specific TCR in complex with its cognate antigen |
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