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T Cell Allorecognition via Molecular Mimicry
T cells often alloreact with foreign human leukocyte antigens (HLA). Here we showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B ∗0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B ∗4402 and HLA-B ∗4405) bound to two different allopeptides. Despite extensiv...
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| Published in: | Immunity (Cambridge, Mass.) Mass.), 2009-12, Vol.31 (6), p.897-908 |
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| creator | Macdonald, Whitney A. Chen, Zhenjun Gras, Stephanie Archbold, Julia K. Tynan, Fleur E. Clements, Craig S. Bharadwaj, Mandvi Kjer-Nielsen, Lars Saunders, Philippa M. Wilce, Matthew C.J. Crawford, Fran Stadinsky, Brian Jackson, David Brooks, Andrew G. Purcell, Anthony W. Kappler, John W. Burrows, Scott R. Rossjohn, Jamie McCluskey, James |
| description | T cells often alloreact with foreign human leukocyte antigens (HLA). Here we showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B
∗0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B
∗4402 and HLA-B
∗4405) bound to two different allopeptides. Despite extensive polymorphism between HLA-B
∗0801, HLA-B
∗4402, and HLA-B
∗4405 and the disparate sequences of the viral and allopeptides, the LC13 TCR engaged these peptide-HLA (pHLA) complexes identically, accommodating mimicry of the viral peptide by the allopeptide. The viral and allopeptides adopted similar conformations only after TCR ligation, revealing an induced-fit mechanism of molecular mimicry. The LC13 T cells did not alloreact against HLA-B
∗4403, and the single residue polymorphism between HLA-B
∗4402 and HLA-B
∗4403 affected the plasticity of the allopeptide, revealing that molecular mimicry was associated with TCR specificity. Accordingly, molecular mimicry that is HLA and peptide dependent is a mechanism for human T cell alloreactivity between disparate cognate and allogeneic pHLA complexes. |
| doi_str_mv | 10.1016/j.immuni.2009.09.025 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_746014054</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S107476130900510X</els_id><sourcerecordid>746014054</sourcerecordid><originalsourceid>FETCH-LOGICAL-c494t-9c544f2f54b760b95ca25d42c2b4046dae62a1dcd3ed87d6f8bb83497f3ed2f73</originalsourceid><addsrcrecordid>eNqFkF1LwzAUhoMoTqf_QKTghTd25uMkbW-EMfyCDW_mdWiTVDLaZibrYP_elE0vvFA4kBCe95ycB6ErgicEE3G_mti27Ts7oRgXk6EoP0JnBBdZCiTHx8M9gzQThI3QeQgrjAnwAp-iUYwIAMjP0N0ymZmmSaZN47xR7qOzG-u6ZGvLZOEao_qm9MnCtlb53QU6qcsmmMvDOUbvT4_L2Us6f3t-nU3nqYICNmmhOEBNaw5VJnBVcFVSroEqWgEGoUsjaEm00szoPNOizqsqZ1BkdXygdcbG6Hbfd-3dZ2_CRrY2qPjNsjOuDzIDEVfBHP4nGVDGWM4iefOLXLned3ENSTgGKnJKRKRgTynvQvCmlmtv29LvJMFy0C5Xcq9dDtrlUJTH2PWheV-1Rv-Evj1H4GEPmKhta42XQVnTKaNttL6R2tm_J3wB3LKTOA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1504268216</pqid></control><display><type>article</type><title>T Cell Allorecognition via Molecular Mimicry</title><source>BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS</source><creator>Macdonald, Whitney A. ; Chen, Zhenjun ; Gras, Stephanie ; Archbold, Julia K. ; Tynan, Fleur E. ; Clements, Craig S. ; Bharadwaj, Mandvi ; Kjer-Nielsen, Lars ; Saunders, Philippa M. ; Wilce, Matthew C.J. ; Crawford, Fran ; Stadinsky, Brian ; Jackson, David ; Brooks, Andrew G. ; Purcell, Anthony W. ; Kappler, John W. ; Burrows, Scott R. ; Rossjohn, Jamie ; McCluskey, James</creator><creatorcontrib>Macdonald, Whitney A. ; Chen, Zhenjun ; Gras, Stephanie ; Archbold, Julia K. ; Tynan, Fleur E. ; Clements, Craig S. ; Bharadwaj, Mandvi ; Kjer-Nielsen, Lars ; Saunders, Philippa M. ; Wilce, Matthew C.J. ; Crawford, Fran ; Stadinsky, Brian ; Jackson, David ; Brooks, Andrew G. ; Purcell, Anthony W. ; Kappler, John W. ; Burrows, Scott R. ; Rossjohn, Jamie ; McCluskey, James</creatorcontrib><description>T cells often alloreact with foreign human leukocyte antigens (HLA). Here we showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B
∗0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B
∗4402 and HLA-B
∗4405) bound to two different allopeptides. Despite extensive polymorphism between HLA-B
∗0801, HLA-B
∗4402, and HLA-B
∗4405 and the disparate sequences of the viral and allopeptides, the LC13 TCR engaged these peptide-HLA (pHLA) complexes identically, accommodating mimicry of the viral peptide by the allopeptide. The viral and allopeptides adopted similar conformations only after TCR ligation, revealing an induced-fit mechanism of molecular mimicry. The LC13 T cells did not alloreact against HLA-B
∗4403, and the single residue polymorphism between HLA-B
∗4402 and HLA-B
∗4403 affected the plasticity of the allopeptide, revealing that molecular mimicry was associated with TCR specificity. Accordingly, molecular mimicry that is HLA and peptide dependent is a mechanism for human T cell alloreactivity between disparate cognate and allogeneic pHLA complexes.</description><identifier>ISSN: 1074-7613</identifier><identifier>EISSN: 1097-4180</identifier><identifier>DOI: 10.1016/j.immuni.2009.09.025</identifier><identifier>PMID: 20064448</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cell Line ; Epstein-Barr Virus Nuclear Antigens - immunology ; HLA-B Antigens - immunology ; HLA-B8 Antigen ; Humans ; Jurkat Cells ; Ligands ; Lymphocyte Activation - immunology ; Lymphocytes ; Molecular Mimicry - immunology ; MOLIMMUNO ; Peptides ; Peptides - chemistry ; Peptides - immunology ; PROTEINS ; Receptors, Antigen, T-Cell - chemistry ; Receptors, Antigen, T-Cell - immunology ; Receptors, Antigen, T-Cell - metabolism ; STRUCTURE ; T cell receptors ; T-Lymphocytes - immunology ; T-Lymphocytes - metabolism ; Transfection ; Transplants & implants</subject><ispartof>Immunity (Cambridge, Mass.), 2009-12, Vol.31 (6), p.897-908</ispartof><rights>2009 Elsevier Inc.</rights><rights>Copyright 2009 Elsevier Inc. All rights reserved.</rights><rights>Copyright Elsevier Limited Dec 18, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c494t-9c544f2f54b760b95ca25d42c2b4046dae62a1dcd3ed87d6f8bb83497f3ed2f73</citedby><cites>FETCH-LOGICAL-c494t-9c544f2f54b760b95ca25d42c2b4046dae62a1dcd3ed87d6f8bb83497f3ed2f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20064448$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Macdonald, Whitney A.</creatorcontrib><creatorcontrib>Chen, Zhenjun</creatorcontrib><creatorcontrib>Gras, Stephanie</creatorcontrib><creatorcontrib>Archbold, Julia K.</creatorcontrib><creatorcontrib>Tynan, Fleur E.</creatorcontrib><creatorcontrib>Clements, Craig S.</creatorcontrib><creatorcontrib>Bharadwaj, Mandvi</creatorcontrib><creatorcontrib>Kjer-Nielsen, Lars</creatorcontrib><creatorcontrib>Saunders, Philippa M.</creatorcontrib><creatorcontrib>Wilce, Matthew C.J.</creatorcontrib><creatorcontrib>Crawford, Fran</creatorcontrib><creatorcontrib>Stadinsky, Brian</creatorcontrib><creatorcontrib>Jackson, David</creatorcontrib><creatorcontrib>Brooks, Andrew G.</creatorcontrib><creatorcontrib>Purcell, Anthony W.</creatorcontrib><creatorcontrib>Kappler, John W.</creatorcontrib><creatorcontrib>Burrows, Scott R.</creatorcontrib><creatorcontrib>Rossjohn, Jamie</creatorcontrib><creatorcontrib>McCluskey, James</creatorcontrib><title>T Cell Allorecognition via Molecular Mimicry</title><title>Immunity (Cambridge, Mass.)</title><addtitle>Immunity</addtitle><description>T cells often alloreact with foreign human leukocyte antigens (HLA). Here we showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B
∗0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B
∗4402 and HLA-B
∗4405) bound to two different allopeptides. Despite extensive polymorphism between HLA-B
∗0801, HLA-B
∗4402, and HLA-B
∗4405 and the disparate sequences of the viral and allopeptides, the LC13 TCR engaged these peptide-HLA (pHLA) complexes identically, accommodating mimicry of the viral peptide by the allopeptide. The viral and allopeptides adopted similar conformations only after TCR ligation, revealing an induced-fit mechanism of molecular mimicry. The LC13 T cells did not alloreact against HLA-B
∗4403, and the single residue polymorphism between HLA-B
∗4402 and HLA-B
∗4403 affected the plasticity of the allopeptide, revealing that molecular mimicry was associated with TCR specificity. Accordingly, molecular mimicry that is HLA and peptide dependent is a mechanism for human T cell alloreactivity between disparate cognate and allogeneic pHLA complexes.</description><subject>Cell Line</subject><subject>Epstein-Barr Virus Nuclear Antigens - immunology</subject><subject>HLA-B Antigens - immunology</subject><subject>HLA-B8 Antigen</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>Ligands</subject><subject>Lymphocyte Activation - immunology</subject><subject>Lymphocytes</subject><subject>Molecular Mimicry - immunology</subject><subject>MOLIMMUNO</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - immunology</subject><subject>PROTEINS</subject><subject>Receptors, Antigen, T-Cell - chemistry</subject><subject>Receptors, Antigen, T-Cell - immunology</subject><subject>Receptors, Antigen, T-Cell - metabolism</subject><subject>STRUCTURE</subject><subject>T cell receptors</subject><subject>T-Lymphocytes - immunology</subject><subject>T-Lymphocytes - metabolism</subject><subject>Transfection</subject><subject>Transplants & implants</subject><issn>1074-7613</issn><issn>1097-4180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkF1LwzAUhoMoTqf_QKTghTd25uMkbW-EMfyCDW_mdWiTVDLaZibrYP_elE0vvFA4kBCe95ycB6ErgicEE3G_mti27Ts7oRgXk6EoP0JnBBdZCiTHx8M9gzQThI3QeQgrjAnwAp-iUYwIAMjP0N0ymZmmSaZN47xR7qOzG-u6ZGvLZOEao_qm9MnCtlb53QU6qcsmmMvDOUbvT4_L2Us6f3t-nU3nqYICNmmhOEBNaw5VJnBVcFVSroEqWgEGoUsjaEm00szoPNOizqsqZ1BkdXygdcbG6Hbfd-3dZ2_CRrY2qPjNsjOuDzIDEVfBHP4nGVDGWM4iefOLXLned3ENSTgGKnJKRKRgTynvQvCmlmtv29LvJMFy0C5Xcq9dDtrlUJTH2PWheV-1Rv-Evj1H4GEPmKhta42XQVnTKaNttL6R2tm_J3wB3LKTOA</recordid><startdate>20091218</startdate><enddate>20091218</enddate><creator>Macdonald, Whitney A.</creator><creator>Chen, Zhenjun</creator><creator>Gras, Stephanie</creator><creator>Archbold, Julia K.</creator><creator>Tynan, Fleur E.</creator><creator>Clements, Craig S.</creator><creator>Bharadwaj, Mandvi</creator><creator>Kjer-Nielsen, Lars</creator><creator>Saunders, Philippa M.</creator><creator>Wilce, Matthew C.J.</creator><creator>Crawford, Fran</creator><creator>Stadinsky, Brian</creator><creator>Jackson, David</creator><creator>Brooks, Andrew G.</creator><creator>Purcell, Anthony W.</creator><creator>Kappler, John W.</creator><creator>Burrows, Scott R.</creator><creator>Rossjohn, Jamie</creator><creator>McCluskey, James</creator><general>Elsevier Inc</general><general>Elsevier Limited</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20091218</creationdate><title>T Cell Allorecognition via Molecular Mimicry</title><author>Macdonald, Whitney A. ; Chen, Zhenjun ; Gras, Stephanie ; Archbold, Julia K. ; Tynan, Fleur E. ; Clements, Craig S. ; Bharadwaj, Mandvi ; Kjer-Nielsen, Lars ; Saunders, Philippa M. ; Wilce, Matthew C.J. ; Crawford, Fran ; Stadinsky, Brian ; Jackson, David ; Brooks, Andrew G. ; Purcell, Anthony W. ; Kappler, John W. ; Burrows, Scott R. ; Rossjohn, Jamie ; McCluskey, James</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-9c544f2f54b760b95ca25d42c2b4046dae62a1dcd3ed87d6f8bb83497f3ed2f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Cell Line</topic><topic>Epstein-Barr Virus Nuclear Antigens - immunology</topic><topic>HLA-B Antigens - immunology</topic><topic>HLA-B8 Antigen</topic><topic>Humans</topic><topic>Jurkat Cells</topic><topic>Ligands</topic><topic>Lymphocyte Activation - immunology</topic><topic>Lymphocytes</topic><topic>Molecular Mimicry - immunology</topic><topic>MOLIMMUNO</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - immunology</topic><topic>PROTEINS</topic><topic>Receptors, Antigen, T-Cell - chemistry</topic><topic>Receptors, Antigen, T-Cell - immunology</topic><topic>Receptors, Antigen, T-Cell - metabolism</topic><topic>STRUCTURE</topic><topic>T cell receptors</topic><topic>T-Lymphocytes - immunology</topic><topic>T-Lymphocytes - metabolism</topic><topic>Transfection</topic><topic>Transplants & implants</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Macdonald, Whitney A.</creatorcontrib><creatorcontrib>Chen, Zhenjun</creatorcontrib><creatorcontrib>Gras, Stephanie</creatorcontrib><creatorcontrib>Archbold, Julia K.</creatorcontrib><creatorcontrib>Tynan, Fleur E.</creatorcontrib><creatorcontrib>Clements, Craig S.</creatorcontrib><creatorcontrib>Bharadwaj, Mandvi</creatorcontrib><creatorcontrib>Kjer-Nielsen, Lars</creatorcontrib><creatorcontrib>Saunders, Philippa M.</creatorcontrib><creatorcontrib>Wilce, Matthew C.J.</creatorcontrib><creatorcontrib>Crawford, Fran</creatorcontrib><creatorcontrib>Stadinsky, Brian</creatorcontrib><creatorcontrib>Jackson, David</creatorcontrib><creatorcontrib>Brooks, Andrew G.</creatorcontrib><creatorcontrib>Purcell, Anthony W.</creatorcontrib><creatorcontrib>Kappler, John W.</creatorcontrib><creatorcontrib>Burrows, Scott R.</creatorcontrib><creatorcontrib>Rossjohn, Jamie</creatorcontrib><creatorcontrib>McCluskey, James</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Immunity (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Macdonald, Whitney A.</au><au>Chen, Zhenjun</au><au>Gras, Stephanie</au><au>Archbold, Julia K.</au><au>Tynan, Fleur E.</au><au>Clements, Craig S.</au><au>Bharadwaj, Mandvi</au><au>Kjer-Nielsen, Lars</au><au>Saunders, Philippa M.</au><au>Wilce, Matthew C.J.</au><au>Crawford, Fran</au><au>Stadinsky, Brian</au><au>Jackson, David</au><au>Brooks, Andrew G.</au><au>Purcell, Anthony W.</au><au>Kappler, John W.</au><au>Burrows, Scott R.</au><au>Rossjohn, Jamie</au><au>McCluskey, James</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>T Cell Allorecognition via Molecular Mimicry</atitle><jtitle>Immunity (Cambridge, Mass.)</jtitle><addtitle>Immunity</addtitle><date>2009-12-18</date><risdate>2009</risdate><volume>31</volume><issue>6</issue><spage>897</spage><epage>908</epage><pages>897-908</pages><issn>1074-7613</issn><eissn>1097-4180</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><notes>ObjectType-Article-2</notes><notes>ObjectType-Feature-1</notes><abstract>T cells often alloreact with foreign human leukocyte antigens (HLA). Here we showed the LC13 T cell receptor (TCR), selected for recognition on self-HLA-B
∗0801 bound to a viral peptide, alloreacts with B44 allotypes (HLA-B
∗4402 and HLA-B
∗4405) bound to two different allopeptides. Despite extensive polymorphism between HLA-B
∗0801, HLA-B
∗4402, and HLA-B
∗4405 and the disparate sequences of the viral and allopeptides, the LC13 TCR engaged these peptide-HLA (pHLA) complexes identically, accommodating mimicry of the viral peptide by the allopeptide. The viral and allopeptides adopted similar conformations only after TCR ligation, revealing an induced-fit mechanism of molecular mimicry. The LC13 T cells did not alloreact against HLA-B
∗4403, and the single residue polymorphism between HLA-B
∗4402 and HLA-B
∗4403 affected the plasticity of the allopeptide, revealing that molecular mimicry was associated with TCR specificity. Accordingly, molecular mimicry that is HLA and peptide dependent is a mechanism for human T cell alloreactivity between disparate cognate and allogeneic pHLA complexes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20064448</pmid><doi>10.1016/j.immuni.2009.09.025</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Immunity (Cambridge, Mass.), 2009-12, Vol.31 (6), p.897-908 |
| issn | 1074-7613 1097-4180 |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Cell Line Epstein-Barr Virus Nuclear Antigens - immunology HLA-B Antigens - immunology HLA-B8 Antigen Humans Jurkat Cells Ligands Lymphocyte Activation - immunology Lymphocytes Molecular Mimicry - immunology MOLIMMUNO Peptides Peptides - chemistry Peptides - immunology PROTEINS Receptors, Antigen, T-Cell - chemistry Receptors, Antigen, T-Cell - immunology Receptors, Antigen, T-Cell - metabolism STRUCTURE T cell receptors T-Lymphocytes - immunology T-Lymphocytes - metabolism Transfection Transplants & implants |
| title | T Cell Allorecognition via Molecular Mimicry |
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