Evidence map›Paper›PMID 21454588›Full record

ArticleThe Journal of biological chemistry2011

Adenovirus E3-19K proteins of different serotypes and subgroups have similar, yet distinct, immunomodulatory functions toward major histocompatibility class I molecules.

Jie Fu, Lenong Li, Marlene Bouvier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. Contribution to pathogenesis of accessory proteins of deadly human coronaviruses.Frontiers in cellular and infection microbiology · 2023
    Review
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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

3 authors at 2 institutions in 1 country.

Jie FuDepartment of Microbiology and Immunology, University of Illinois, College of Medicine, Chicago, Illinois 60612, USA.
Lenong Li
Marlene Bouvier
University of Illinois Chicago · USIllinois College · US

Funding

CTSA INFRASTRUCTURE FOR PEDIATRIC RESEARCHUL1RR029879 · NCRR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MAZZONE, THEODORE · 2009 to 2011
$11.0M
IN VITRO FOLDING AND ASSEMBLY OF CLASS I MHC MOLECULESR01AI045070 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BOUVIER, MARLENE · 2000 to 2011
$2.5M
In vitro folding and assembly of class I MHC moleculesR56AI045070 · NIAID · UNIVERSITY OF CONNECTICUT STORRS · PI BOUVIER, MARLENE · 2006 to 2006
$325k
NCRR NIH HHS UL1 RR029879NCRR NIH HHS UL1RR029879NIAID NIH HHS AI045070NIAID NIH HHS R01 AI045070NIAID NIH HHS R56 AI045070
6 · The paper itself

Abstract

Our understanding of the mechanism by which the E3-19K protein from adenovirus (Ad) targets major histocompatibility complex (MHC) class I molecules for retention in the endoplasmic reticulum is derived largely from studies of Ad serotype 2 (subgroup C). It is not well understood to what extent observations on the Ad2 E3-19K/MHC I association can be generalized to E3-19K proteins of other serotypes and subgroups. The low levels of amino acid sequence homology between E3-19K proteins suggest that these proteins are likely to manifest distinct MHC I binding properties. This information is important as the E3-19K/MHC I interaction is thought to play a critical role in enabling Ads to cause persistent infections. Here, we characterized interaction between E3-19K proteins of serotypes 7 and 35 (subgroup B), 5 (subgroup C), 37 (subgroup D), and 4 (subgroup E) and a panel of HLA-A, -B, and -C molecules using native gel, surface plasmon resonance (SPR), and flow cytometry. Results show that all E3-19K proteins exhibited allele specificity toward HLA-A and -B molecules; this was less evident for Ad37 E3-19K. The allele specificity for HLA-A molecules was remarkably similar for different serotypes of subgroup B as well as subgroup C. Interestingly, all E3-19K proteins characterized also exhibited MHC I locus specificity. Importantly, we show that Lys(91) in the conserved region of Ad2 E3-19K targets the C terminus of the α2-helix (MHC residue 177) on MHC class I molecules. From our data, we propose a model of interaction between E3-19K and MHC class I molecules.

Indexed as

AdenoviridaeAdenovirus E3 ProteinsAdenovirus Early ProteinsCell LineHLA-A AntigensHLA-B AntigensHumansProtein Structure, SecondarySpecies SpecificityAdenovirus E3 ProteinsAdenovirus Early ProteinsHLA-A AntigensHLA-B Antigens

Identifiers

PMID21454588
PMCPMC3093838
OpenAlexW1991825344

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.