Evidence map›Paper›PMID 11602636›Full record

ArticleThe Journal of experimental medicine2001

Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway.

G Lautscham, S Mayrhofer, G Taylor, T Haigh, A Leese, A Rickinson, N Blake

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  6. Epstein-Barr virus microRNAs reduce immune surveillance by virus-specific CD8+ T cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
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  8. Review
  9. Review
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  15. Generation of MHC class I ligands in the secretory and vesicular pathways.Cellular and molecular life sciences : CMLS · 2011
    Review
  16. Article
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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

7 authors at 3 institutions in 1 country.

G LautschamCancer Research Campaign Institute for Cancer Studies and Medical Research Council Centre for Immune Regulation, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
S Mayrhofer
G Taylor
T Haigh
A Leese
A Rickinson
N Blake
Medical Research Council · GBUniversity of Birmingham · GBImmune Regulation (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) latent membrane protein (LMP)2 is a multiple membrane spanning molecule which lacks ectodomains projecting into the lumen of the endoplasmic reticulum (ER). Human CD8(+) cytotoxic T lymphocytes (CTL)s recognize a number of epitopes within LMP2. Assays with epitope-specific CTLs in two different cell backgrounds lacking the transporter associated with antigen processing (TAP) consistently show that some, but not all, LMP2 epitopes are presented in a TAP-independent manner. However, unlike published examples of TAP-independent processing from endogenously expressed antigens, presentation of TAP-independent LMP2 epitopes was abrogated by inhibition of proteasomal activity. We found a clear correlation between hydrophobicity of the LMP2 epitope sequence and TAP independence, and experiments with vaccinia minigene constructs expressing cytosolic epitope peptides confirmed that these more hydrophobic peptides were selectively able to access the HLA class I pathway in TAP-negative cells. Furthermore, the TAP-independent phenotype of particular epitope sequences did not require membrane location of the source antigen since (i) TAP-independent LMP2 epitopes inserted into an EBV nuclear antigen and (ii) hydrophobic epitope sequences native to EBV nuclear antigens were both presented in TAP-negative cells. We infer that there is a proteasome-dependent, TAP-independent pathway of antigen presentation which hydrophobic epitopes can selectively access.

Indexed as

Antigen PresentationATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3Cell Line, TransformedCysteine EndopeptidasesCysteine Proteinase InhibitorsEpithelial CellsEpitope MappingEpitopes, T-LymphocyteHerpesvirus 4, HumanHLA-A24 AntigenHLA-A AntigensHLA-B27 AntigenHLA-B40 AntigenHLA-B AntigensATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3Cysteine EndopeptidasesCysteine Proteinase InhibitorsEBV-associated membrane antigen, Epstein-Barr virusEpitopes, T-LymphocyteHLA-A24 AntigenHLA-A AntigensHLA-B27 AntigenHLA-B40 AntigenHLA-B AntigensMultienzyme ComplexesNuclear ProteinsProteasome Endopeptidase ComplexTAP1 protein, humanTAP2 protein, humanViral Matrix Proteins

Identifiers

PMID11602636
PMCPMC2193515
OpenAlexW2096309940

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.