Evidence map›Paper›PMID 15793001›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Varicelloviruses avoid T cell recognition by UL49.5-mediated inactivation of the transporter associated with antigen processing.

Danijela Koppers-Lalic, Eric A J Reits, Maaike E Ressing, Andrea D Lipinska, Rupert Abele, Joachim Koch, Marisa Marcondes Rezende, Pieter Admiraal, Daphne van Leeuwen, Krystyna Bienkowska-Szewczyk and 5 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
9.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

77 citing papers in PubMed, 190 citations in OpenAlex.

  1. Structurally diverse viral inhibitors converge on a shared mechanism to stall the antigen transporter TAP.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. A Structural Atlas of TAP Inhibition by Herpesviruses and Poxviruses.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. The herpesvirus UL49.5 protein hijacks a cellular C-degron pathway to drive TAP transporter degradation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 1 institution in 2 countries.

Danijela Koppers-LalicDepartment of Medical Microbiology, Leiden University Medical Center, 2300 RC, Leiden, The Netherlands.
Eric A J Reits
Maaike E Ressing
Andrea D Lipinska
Rupert Abele
Joachim Koch
Marisa Marcondes Rezende
Pieter Admiraal
Daphne van Leeuwen
Krystyna Bienkowska-Szewczyk
Thomas C Mettenleiter
Frans A M Rijsewijk
Robert Tampé
Jacques Neefjes
Emmanuel J H J Wiertz
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3Biological Transport, ActiveCell LineEndoplasmic ReticulumHistocompatibility Antigens Class IHumansMolecular Sequence DataProteasome Endopeptidase ComplexProtein BindingRecombinant Fusion ProteinsT-Lymphocytes, CytotoxicAdenosine TriphosphateATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3Histocompatibility Antigens Class IProteasome Endopeptidase ComplexRecombinant Fusion ProteinsTAP1 protein, humanTAP2 protein, humanUL49.5 protein, bovine herpesvirus type 1Viral Envelope Proteins

Identifiers

PMID15793001
PMCPMC555605
OpenAlexW2144526193

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.