No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes

Basler, Michael; Gröttrup, Marcus

No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes

Dateien

Basler_220108.pdfGröße: 241.61 KBDownloads: 288

Datum

2007

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

European Journal of Immunology. 2007, 37(4), pp. 896-904. ISSN 0014-2980. eISSN 1521-4141. Available under: doi: 10.1002/eji.200636372

Zusammenfassung

The proteasome is critically involved in the production of MHC class I-restricted T cell epitopes. Approximately 20% of all peptides generated by the proteasome are too large for direct presentation by MHC class I molecules. Reits et al. (Immunity 2004. 20:495–506) suggested that a major portion of proteasomal products are larger than 15 amino acids and require further degradation by the tripeptidyl peptidase II (TPPII) before becoming ligands of MHC class I molecules. Using the well-characterized lymphocytic choriomeningitis virus (LCMV) model, the role of TPPII in the processing of several LCMV-derived T cell epitopes was investigated. In contrast to Reits' proposal, TPPII inhibition and TPPII overexpression experiments revealed that five out of six LCMV-derived CD8+ T cell epitopes were not affected by inhibition of TPPII, while one epitope (GP276) was slightly reduced upon TPPII overexpression. Additionally, we demonstrated that the processing of two epitopes derived from ovalbumin and murine cytomegalovirus were not altered by TPPII inhibition. We propose that TPPII is not generally required for the production of MHC class I peptides, but the presentation of some peptides can be negatively affected by TPPII.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Antigen processing, Cytotoxic T cells, Proteasome

Zitieren

ISO 690

BASLER, Michael, Marcus GRÖTTRUP, 2007. No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes. In: European Journal of Immunology. 2007, 37(4), pp. 896-904. ISSN 0014-2980. eISSN 1521-4141. Available under: doi: 10.1002/eji.200636372

BibTex

@article{Basler2007-04essen-22010,
  year={2007},
  doi={10.1002/eji.200636372},
  title={No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes},
  number={4},
  volume={37},
  issn={0014-2980},
  journal={European Journal of Immunology},
  pages={896--904},
  author={Basler, Michael and Gröttrup, Marcus}
}

RDF

<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/22010">
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/22010/2/Basler_220108.pdf"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/22010"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/22010/2/Basler_220108.pdf"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-28T10:27:34Z</dcterms:available>
    <dcterms:abstract xml:lang="eng">The proteasome is critically involved in the production of MHC class I-restricted T cell epitopes. Approximately 20% of all peptides generated by the proteasome are too large for direct presentation by MHC class I molecules. Reits et al. (Immunity 2004. 20:495–506) suggested that a major portion of proteasomal products are larger than 15 amino acids and require further degradation by the tripeptidyl peptidase II (TPPII) before becoming ligands of MHC class I molecules. Using the well-characterized lymphocytic choriomeningitis virus (LCMV) model, the role of TPPII in the processing of several LCMV-derived T cell epitopes was investigated. In contrast to Reits' proposal, TPPII inhibition and TPPII overexpression experiments revealed that five out of six LCMV-derived CD8+ T cell epitopes were not affected by inhibition of TPPII, while one epitope (GP276) was slightly reduced upon TPPII overexpression. Additionally, we demonstrated that the processing of two epitopes derived from ovalbumin and murine cytomegalovirus were not altered by TPPII inhibition. We propose that TPPII is not generally required for the production of MHC class I peptides, but the presentation of some peptides can be negatively affected by TPPII.</dcterms:abstract>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:rights>terms-of-use</dc:rights>
    <dcterms:bibliographicCitation>European Journal of Immunology ; 37 (2007), 4. - S. 896-904</dcterms:bibliographicCitation>
    <dc:creator>Gröttrup, Marcus</dc:creator>
    <dcterms:issued>2007-04</dcterms:issued>
    <dc:language>eng</dc:language>
    <dcterms:title>No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes</dcterms:title>
    <dc:contributor>Basler, Michael</dc:contributor>
    <dc:contributor>Gröttrup, Marcus</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-03-28T10:27:34Z</dc:date>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Basler, Michael</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja