Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 347690
Title Varicelloviruses avoid T cell recognition by UL49.5-mediated inactivation of the transporter associated with antigen processing
Author(s) Koppers-Lalic, D.; Reits, E.A.; Ressing, M.E.; Lipinska, A.D.; Abele, R.; Koch, J.; Marcondes Rezende, M.; Admiraal, P.; Leeuwen, D.; Bienkowska-Szewczyk, K.; Mettenleiter, T.C.; Rijsewijk, F.A.M.; Tampe, R.; Neefjes, J.; Wiertz, E.J.
Source Proceedings of the National Academy of Sciences of the United States of America 102 (2005)14. - ISSN 0027-8424 - p. 5144 - 5149.
Department(s) ID - Infectieziekten
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) class-i expression - disulfide-linked complex - peptide-loading complex - virus protein icp47 - endoplasmic-reticulum - equine herpesvirus-1 - glycoprotein-m - transmembrane domains - molecular-mechanism - down-regulation
Abstract Detection and elimination of virus-infected cells by cytotoxic T lymphocytes depends on recognition of virus-derived peptides presented by MHC class I molecules. A critical step in this process is the translocation of peptides from the cytoplasm into the endoplasmic reticulum by the transporter associated with antigen processing (TAP). Here, we identified the bovine herpesvirus 1-encoded UL49.5 protein as a potent inhibitor of TAP. The expression of UL49.5 results in down-regulation of MHC class I molecules at the cell surface and inhibits detection and lysis of the cells by cytotoxic T lymphocytes. UL49.5 homologs encoded by two other varicelloviruses, pseudorabies-virus and equine herpesvirus 1, also block TAP. Homologs of UL49.5 are widely present in herpesviruses, acting as interaction partners for glycoprotein M, but in several varicelloviruses UL49.5 has uniquely evolved additional functions that mediate its participation in TAP inhibition. Inactivation of TAP by UL49.5 involves two events: inhibition of peptide transport through a conformational arrest of the transporter and degradation of TAP by proteasomes. UL49.5 is degraded along with TAP via a reaction that requires the cytoplasmic tail of UL49.5. Thus, UL49.5 represents a unique immune evasion protein that inactivates TAP through a unique two-tiered process
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