Evidence map›Paper›PMID 12829816›Full record

ArticleJournal of virology2003

Mutations within the ADP (E3-11.6K) protein alter processing and localization of ADP and the kinetics of cell lysis of adenovirus-infected cells.

Ann E Tollefson, Abraham Scaria, Baoling Ying, William S M Wold

Abstract read
In one paragraph

Article in Journal of virology, 2003. 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
1.2field-weighted citation impact, top 20% 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, 34 citations in OpenAlex.

  1. Trial
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  9. Adenovirus i-leader truncation bioselected against cancer-associated fibroblasts to overcome tumor stromal barriers.Molecular therapy : the journal of the American Society of Gene Therapy · 2012
    Article
  10. Article
  11. Article
  12. Verapamil enhances the antitumoral efficacy of oncolytic adenoviruses.Molecular therapy : the journal of the American Society of Gene Therapy · 2010
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Development of a prototype immunochromatographic test for rapid diagnosis of respiratory adenovirus infection.The Brazilian journal of infectious diseases : an official publication of the Brazilian Society of Infectious Diseases
    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

4 authors at 1 institution in 1 country.

Ann E TollefsonDepartment of Molecular Microbiology and Immunology, St. Louis University Health Sciences Center, 1402 S. Grand Boulevard, St. Louis, MO 63104, USA.
Abraham Scaria
Baoling Ying
William S M Wold
Saint Louis University · US

Funding

ADENOVIRUS E3 PROTEINS AND TUMOR NECROSIS FACTORR01CA058538 · NCI · SAINT LOUIS UNIVERSITY · PI WOLD, WILLIAM SM · 1993 to 2001
$531k
ADENOVIRUS DEATH PROTEINR01CA071704 · NCI · SAINT LOUIS UNIVERSITY · PI WOLD, WILLIAM SM · 1996 to 2000
$306k
ADENOVIRUS TWO CODED EARLY GLYCOPROTEINR01CA024710 · NCI · SAINT LOUIS UNIVERSITY · PI WOLD, WILLIAM SM · 1985 to 1997
–
NCI NIH HHS CA 24710NCI NIH HHS CA 58538NCI NIH HHS CA 71704
6 · The paper itself

Abstract

ADP (also known as E3-11.6K protein) is synthesized abundantly in late adenovirus infection and is required for efficient lysis of infected cells and release of viral progeny at the end of the viral replication cycle. ADP is a type III bitopic N(endo)C(exo) nuclear membrane and Golgi glycoprotein that is produced at high levels in late adenovirus infection (>24 h postinfection). We show pulse-chase and other studies indicating that ADP undergoes a complex process of N- and O-linked glycosylation and proteolytic cleavage. In order to further characterize ADP, a series of 23 deletion and point mutations has been constructed in the adenovirus serotype 2 adp gene and then built into a wild-type adenovirus background. These mutants were analyzed for processing and intracellular localization of ADP. Mutation of the single predicted N glycosylation site eliminated N glycosylation. Deletion of a region in ADP rich in serine and threonine residues reduced O glycosylation. In general, mutations within the lumenal domain of ADP resulted in lower protein stability; immunofluorescence assays indicated that these ADPs were primarily present in the Golgi apparatus. Viruses with mutations within the cytoplasmic-nucleoplasmic domain of ADP showed normal glycosylation patterns and protein abundance for ADP, but the protein was often found throughout cellular membranes rather than being localized specifically to the nuclear membrane and Golgi apparatus. The ADP virus mutants were analyzed by cell viability assays to determine the kinetics of cell lysis following infection of human A549 cells. In general, viruses with mutations within the lumenal domain of ADP display greatly reduced efficiencies of cell lysis. Viruses with large deletions in the cytoplasmic-nucleoplasmic domain of ADP retain much of their ability to lyse infected cells.

Indexed as

Cell DeathMutationAdenovirus E3 ProteinsAdenoviruses, HumanAnimalsCHO CellsCricetinaeFluorescent Antibody TechniqueGene DeletionGenes, ViralGlycosylationGolgi ApparatusHumansKineticsPoint MutationProtein Processing, Post-Translationaladenovirus death protein, AdenovirusAdenovirus E3 Proteins

Identifiers

PMID12829816
PMCPMC161948
OpenAlexW2032925373

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.