Evidence map›Paper›PMID 8057424›Full record

ArticleJournal of virology1994

Conserved cysteine residues within the E3/19K protein of adenovirus type 2 are essential for binding to major histocompatibility complex antigens.

M Sester, H G Burgert

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  4. A unique secreted adenovirus E3 protein binds to the leukocyte common antigen CD45 and modulates leukocyte functions.Proceedings of the National Academy of Sciences of the United States of America · 2013
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  8. Review
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  14. Review
  15. The adenovirus E3/10.4K-14.5K proteins down-modulate the apoptosis receptor Fas/Apo-1 by inducing its internalization.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  16. Human cytomegalovirus inhibits antigen presentation by a sequential multistep process.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  17. Article
  18. Article
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

2 authors at 1 institution in 1 country.

M SesterHans-Spemann-Laboratorium, Max-Planck-Institut für Immunobiologie, Freiburg, Germany.
H G Burgert
Max Planck Institute of Immunobiology and Epigenetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E3/19K protein of human adenovirus type 2 is a resident transmembrane glycoprotein of the endoplasmic reticulum. Its capacity to associate with class I histocompatibility (MHC) antigens abrogates cell surface expression and the antigen presentation function of MHC antigens. At present, it is unclear exactly which structure of the E3/19K protein mediates binding to MHC molecules. Apart from a stretch of approximately 20 conserved amino acids in front of the transmembrane segment, E3/19K molecules from different adenovirus subgroups (B and C) share little homology. Remarkably, the majority of cysteines are conserved. In this report, we examined the importance of cysteine residues for the structure and function of E3/19K. We show that E3/19K contains intramolecular disulfide bonds. By using site-directed mutagenesis, individual cysteines were replaced by serines and mutant proteins were stably expressed in 293 cells. On the basis of the differential binding of monoclonal antibody Tw1.3 and cyanogen bromide cleavage experiments, a structural model of E3/19K is proposed, in which Cys-11 and Cys-28 as well as Cys-22 and Cys-83 are linked by disulfide bonds. Both disulfide bonds (all four cysteines) are absolutely critical for the interaction with human MHC antigens. This was demonstrated by three criteria: loss of E3/19K coprecipitation, lack of transport inhibition, and normal cell surface expression of MHC molecules. Mutation of the three other cysteines had no effect. This indicates that a conformational determinant based on two disulfide bonds is crucial for the function of the E3/19K molecule, namely, to bind and to inhibit transport of MHC antigens.

Indexed as

Adenovirus E3 ProteinsAdenoviruses, HumanAmino Acid SequenceBase SequenceCell LineCysteineDisulfidesHistocompatibility Antigens Class IHumansMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesProtein BindingProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidAdenovirus E3 ProteinsCysteineDisulfidesHistocompatibility Antigens Class IOligodeoxyribonucleotides

Identifiers

PMID8057424
PMCPMC236942
OpenAlexW1918393334

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.