Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove
- Autores
- McMurtrey, Curtis; Trolle, Thomas; Sansom, Tiffany; Remesh, Soumya G.; Kaever, Thomas; Bardet, Wilfried; Jackson, Kenneth; McLeod, Rima; Sette, Alessandro; Nielsen, Morten; Zajonc, Dirk M.; Blader, Ira J; Peters, Bjoern; Hildebrand, William
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- HLA class I presentation of pathogen-derived peptide ligands is essential for CD8+ T-cell recognition of Toxoplasma gondii infected cells. Currently, little data exist pertaining to peptides that are presented after T. gondii infection. Herein we purify HLA-A*02:01 complexes from T. gondii infected cells and characterize the peptide ligands using LCMS. We identify 195 T. gondii encoded ligands originating from both secreted and cytoplasmic proteins. Surprisingly, T. gondii ligands are significantly longer than uninfected host ligands, and these longer pathogen-derived peptides maintain a canonical N-terminal binding core yet exhibit a C-terminal extension of 1-30 amino acids. Structural analysis demonstrates that binding of extended peptides opens the HLA class I F' pocket, allowing the C-terminal extension to protrude through one end of the binding groove. In summary, we demonstrate that unrealized structural flexibility makes MHC class I receptive to parasite-derived ligands that exhibit unique C-terminal peptide extensions.
Fil: McMurtrey, Curtis. University of Oklahoma; Estados Unidos
Fil: Trolle, Thomas. Technical University of Denmark; Dinamarca. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Sansom, Tiffany. University at Buffalo; Estados Unidos
Fil: Remesh, Soumya G.. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Kaever, Thomas. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Bardet, Wilfried. University of Oklahoma; Estados Unidos
Fil: Jackson, Kenneth. University of Oklahoma; Estados Unidos
Fil: McLeod, Rima. University of Chicago; Estados Unidos
Fil: Sette, Alessandro. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Nielsen, Morten. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Technical University of Denmark; Dinamarca
Fil: Zajonc, Dirk M.. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Blader, Ira J. University at Buffalo; Estados Unidos
Fil: Peters, Bjoern. La Jolla Institute for Allergy and Immunology; Estados Unidos
Fil: Hildebrand, William. University of Oklahoma; Estados Unidos - Materia
-
Human
Immunology
Infectious disease
Microbiology - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/53616
Ver los metadatos del registro completo
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Toxoplasma gondii peptide ligands open the gate of the HLA class I binding grooveMcMurtrey, CurtisTrolle, ThomasSansom, TiffanyRemesh, Soumya G.Kaever, ThomasBardet, WilfriedJackson, KennethMcLeod, RimaSette, AlessandroNielsen, MortenZajonc, Dirk M.Blader, Ira JPeters, BjoernHildebrand, WilliamHumanImmunologyInfectious diseaseMicrobiologyhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3HLA class I presentation of pathogen-derived peptide ligands is essential for CD8+ T-cell recognition of Toxoplasma gondii infected cells. Currently, little data exist pertaining to peptides that are presented after T. gondii infection. Herein we purify HLA-A*02:01 complexes from T. gondii infected cells and characterize the peptide ligands using LCMS. We identify 195 T. gondii encoded ligands originating from both secreted and cytoplasmic proteins. Surprisingly, T. gondii ligands are significantly longer than uninfected host ligands, and these longer pathogen-derived peptides maintain a canonical N-terminal binding core yet exhibit a C-terminal extension of 1-30 amino acids. Structural analysis demonstrates that binding of extended peptides opens the HLA class I F' pocket, allowing the C-terminal extension to protrude through one end of the binding groove. In summary, we demonstrate that unrealized structural flexibility makes MHC class I receptive to parasite-derived ligands that exhibit unique C-terminal peptide extensions.Fil: McMurtrey, Curtis. University of Oklahoma; Estados UnidosFil: Trolle, Thomas. Technical University of Denmark; Dinamarca. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Sansom, Tiffany. University at Buffalo; Estados UnidosFil: Remesh, Soumya G.. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Kaever, Thomas. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Bardet, Wilfried. University of Oklahoma; Estados UnidosFil: Jackson, Kenneth. University of Oklahoma; Estados UnidosFil: McLeod, Rima. University of Chicago; Estados UnidosFil: Sette, Alessandro. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Nielsen, Morten. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Technical University of Denmark; DinamarcaFil: Zajonc, Dirk M.. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Blader, Ira J. University at Buffalo; Estados UnidosFil: Peters, Bjoern. La Jolla Institute for Allergy and Immunology; Estados UnidosFil: Hildebrand, William. University of Oklahoma; Estados UnidoseLife Sciences Publications2016-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/53616McMurtrey, Curtis; Trolle, Thomas; Sansom, Tiffany; Remesh, Soumya G.; Kaever, Thomas; et al.; Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove; eLife Sciences Publications; eLife; 5; 1-2016; 1-192050-084XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.12556info:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/12556info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:09:47Zoai:ri.conicet.gov.ar:11336/53616instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:09:47.465CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| title |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| spellingShingle |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove McMurtrey, Curtis Human Immunology Infectious disease Microbiology |
| title_short |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| title_full |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| title_fullStr |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| title_full_unstemmed |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| title_sort |
Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove |
| dc.creator.none.fl_str_mv |
McMurtrey, Curtis Trolle, Thomas Sansom, Tiffany Remesh, Soumya G. Kaever, Thomas Bardet, Wilfried Jackson, Kenneth McLeod, Rima Sette, Alessandro Nielsen, Morten Zajonc, Dirk M. Blader, Ira J Peters, Bjoern Hildebrand, William |
| author |
McMurtrey, Curtis |
| author_facet |
McMurtrey, Curtis Trolle, Thomas Sansom, Tiffany Remesh, Soumya G. Kaever, Thomas Bardet, Wilfried Jackson, Kenneth McLeod, Rima Sette, Alessandro Nielsen, Morten Zajonc, Dirk M. Blader, Ira J Peters, Bjoern Hildebrand, William |
| author_role |
author |
| author2 |
Trolle, Thomas Sansom, Tiffany Remesh, Soumya G. Kaever, Thomas Bardet, Wilfried Jackson, Kenneth McLeod, Rima Sette, Alessandro Nielsen, Morten Zajonc, Dirk M. Blader, Ira J Peters, Bjoern Hildebrand, William |
| author2_role |
author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Human Immunology Infectious disease Microbiology |
| topic |
Human Immunology Infectious disease Microbiology |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.3 https://purl.org/becyt/ford/3 |
| dc.description.none.fl_txt_mv |
HLA class I presentation of pathogen-derived peptide ligands is essential for CD8+ T-cell recognition of Toxoplasma gondii infected cells. Currently, little data exist pertaining to peptides that are presented after T. gondii infection. Herein we purify HLA-A*02:01 complexes from T. gondii infected cells and characterize the peptide ligands using LCMS. We identify 195 T. gondii encoded ligands originating from both secreted and cytoplasmic proteins. Surprisingly, T. gondii ligands are significantly longer than uninfected host ligands, and these longer pathogen-derived peptides maintain a canonical N-terminal binding core yet exhibit a C-terminal extension of 1-30 amino acids. Structural analysis demonstrates that binding of extended peptides opens the HLA class I F' pocket, allowing the C-terminal extension to protrude through one end of the binding groove. In summary, we demonstrate that unrealized structural flexibility makes MHC class I receptive to parasite-derived ligands that exhibit unique C-terminal peptide extensions. Fil: McMurtrey, Curtis. University of Oklahoma; Estados Unidos Fil: Trolle, Thomas. Technical University of Denmark; Dinamarca. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Sansom, Tiffany. University at Buffalo; Estados Unidos Fil: Remesh, Soumya G.. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Kaever, Thomas. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Bardet, Wilfried. University of Oklahoma; Estados Unidos Fil: Jackson, Kenneth. University of Oklahoma; Estados Unidos Fil: McLeod, Rima. University of Chicago; Estados Unidos Fil: Sette, Alessandro. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Nielsen, Morten. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Technical University of Denmark; Dinamarca Fil: Zajonc, Dirk M.. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Blader, Ira J. University at Buffalo; Estados Unidos Fil: Peters, Bjoern. La Jolla Institute for Allergy and Immunology; Estados Unidos Fil: Hildebrand, William. University of Oklahoma; Estados Unidos |
| description |
HLA class I presentation of pathogen-derived peptide ligands is essential for CD8+ T-cell recognition of Toxoplasma gondii infected cells. Currently, little data exist pertaining to peptides that are presented after T. gondii infection. Herein we purify HLA-A*02:01 complexes from T. gondii infected cells and characterize the peptide ligands using LCMS. We identify 195 T. gondii encoded ligands originating from both secreted and cytoplasmic proteins. Surprisingly, T. gondii ligands are significantly longer than uninfected host ligands, and these longer pathogen-derived peptides maintain a canonical N-terminal binding core yet exhibit a C-terminal extension of 1-30 amino acids. Structural analysis demonstrates that binding of extended peptides opens the HLA class I F' pocket, allowing the C-terminal extension to protrude through one end of the binding groove. In summary, we demonstrate that unrealized structural flexibility makes MHC class I receptive to parasite-derived ligands that exhibit unique C-terminal peptide extensions. |
| publishDate |
2016 |
| dc.date.none.fl_str_mv |
2016-01 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/53616 McMurtrey, Curtis; Trolle, Thomas; Sansom, Tiffany; Remesh, Soumya G.; Kaever, Thomas; et al.; Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove; eLife Sciences Publications; eLife; 5; 1-2016; 1-19 2050-084X CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/53616 |
| identifier_str_mv |
McMurtrey, Curtis; Trolle, Thomas; Sansom, Tiffany; Remesh, Soumya G.; Kaever, Thomas; et al.; Toxoplasma gondii peptide ligands open the gate of the HLA class I binding groove; eLife Sciences Publications; eLife; 5; 1-2016; 1-19 2050-084X CONICET Digital CONICET |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
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info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.12556 info:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/12556 |
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application/pdf application/pdf application/pdf |
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eLife Sciences Publications |
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eLife Sciences Publications |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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