Evidence map›Paper›PMID 17024246›Full record

ArticleThe Journal of clinical investigation2006

Inhibition of TNF receptor 1 internalization by adenovirus 14.7K as a novel immune escape mechanism.

Wulf Schneider-Brachert, Vladimir Tchikov, Oliver Merkel, Marten Jakob, Cora Hallas, Marie-Luise Kruse, Peter Groitl, Alexander Lehn, Eberhard Hildt, Janka Held-Feindt and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. Adenoviral E3/49K: CD45-targeted immune evasion and therapeutic potential.Frontiers in cellular and infection microbiology · 2026
    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

14 authors at 5 institutions in 2 countries.

Wulf Schneider-BrachertInstitute for Medical Microbiology and Hygiene, University of Regensburg, Regensburg, Germany.
Vladimir Tchikov
Oliver Merkel
Marten Jakob
Cora Hallas
Marie-Luise Kruse
Peter Groitl
Alexander Lehn
Eberhard Hildt
Janka Held-Feindt
Thomas Dobner
Dieter Kabelitz
Martin Krönke
Stefan Schütze
Institute of Immunology · HRUniversity of Regensburg · DEInstitute of Medical Microbiology and Hygiene · DEUniversity of Freiburg · DEUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adenoviral protein E3-14.7K (14.7K) is an inhibitor of TNF-induced apoptosis, but the molecular mechanism underlying this protective effect has not yet been explained exhaustively. TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD), Fas-associated death domain (FADD), and caspase-8 to the death domain of TNF receptor 1 (TNFR1), thereby establishing the death-inducing signaling complex (DISC). Here we report that adenovirus 14.7K protein inhibits ligand-induced TNFR1 internalization. Analysis of purified magnetically labeled TNFR1 complexes from murine and human cells stably transduced with 14.7K revealed that prevention of TNFR1 internalization resulted in inhibition of DISC formation. In contrast, 14.7K did not affect TNF-induced NF-kappaB activation via recruitment of receptor-interacting protein 1 (RIP-1) and TNF receptor-associated factor 2 (TRAF-2). Inhibition of endocytosis by 14.7K was effected by failure of coordinated temporal and spatial assembly of essential components of the endocytic machinery such as Rab5 and dynamin 2 at the site of the activated TNFR1. Furthermore, we found that the same TNF defense mechanisms were instrumental in protecting wild-type adenovirus-infected human cells expressing 14.7K. This study describes a new molecular mechanism implemented by a virus to escape immunosurveillance by selectively targeting TNFR1 endocytosis to prevent TNF-induced DISC formation.

Indexed as

Virus InternalizationAdenoviridaeAdenovirus E3 ProteinsAnimalsApoptosisCell LineDeath Domain Receptor Signaling Adaptor ProteinsEndocytosisHumansMiceNF-kappa BReceptors, Tumor Necrosis FactorTumor Necrosis Factor-alphaAdenovirus E3 ProteinsDeath Domain Receptor Signaling Adaptor ProteinsE3 14.7K protein, AdenovirusNF-kappa BReceptors, Tumor Necrosis FactorTumor Necrosis Factor-alpha

Identifiers

PMID17024246
PMCPMC1590267
OpenAlexW2106254834

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.