Evidence map›Paper›PMID 24227847›Full record

ArticleJournal of virology2014

Processing of the l1 52/55k protein by the adenovirus protease: a new substrate and new insights into virion maturation.

Ana J Pérez-Berná, Walter F Mangel, William J McGrath, Vito Graziano, Jane Flint, Carmen San Martín

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Mysteries of adenovirus packaging.Journal of virology · 2025
    Review
  4. Article
  5. Maturation of Viruses.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Dynamic competition for hexon binding between core protein VII and lytic protein VI promotes adenovirus maturation and entry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Components of Adenovirus Genome Packaging.Frontiers in microbiology · 2016
    Review
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

6 authors at 3 institutions in 2 countries.

Ana J Pérez-BernáDepartment of Macromolecular Structure, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Walter F Mangel
William J McGrath
Vito Graziano
Jane Flint
Carmen San Martín
Brookhaven National Laboratory · USCentro Nacional de Biotecnología · ESPrinceton University · US

Funding

REGULATION OF ADENOVIRUS PROTEINASE BY A PEPTIDE AND DNAR01AI041599 · NIAID · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MANGEL, WALTER F. · 1997 to 2011
$7.4M
TRANSCRIPTIONAL REGULATION OF ADENOVIRUS LATE GENESR01GM037705 · NIGMS · PRINCETON UNIVERSITY · PI FLINT, SARAH JANE · 1987 to 2007
$1.6M
Maturation of adenovirus via a new type of biochemistryR21AI113565 · NIAID · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MANGEL, WALTER F. · 2014 to 2015
$623k
NIAID NIH HHS R01 AI041599NIAID NIH HHS R21 AI113565NIGMS NIH HHS R01 GM037705
6 · The paper itself

Abstract

Late in adenovirus assembly, the viral protease (AVP) becomes activated and cleaves multiple copies of three capsid and three core proteins. Proteolytic maturation is an absolute requirement to render the viral particle infectious. We show here that the L1 52/55k protein, which is present in empty capsids but not in mature virions and is required for genome packaging, is the seventh substrate for AVP. A new estimate on its copy number indicates that there are about 50 molecules of the L1 52/55k protein in the immature virus particle. Using a quasi-in vivo situation, i.e., the addition of recombinant AVP to mildly disrupted immature virus particles, we show that cleavage of L1 52/55k is DNA dependent, as is the cleavage of the other viral precursor proteins, and occurs at multiple sites, many not conforming to AVP consensus cleavage sites. Proteolytic processing of L1 52/55k disrupts its interactions with other capsid and core proteins, providing a mechanism for its removal during viral maturation. Our results support a model in which the role of L1 52/55k protein during assembly consists in tethering the viral core to the icosahedral shell and in which maturation proceeds simultaneously with packaging, before the viral particle is sealed.

Indexed as

Protein Processing, Post-TranslationalVirus AssemblyAdenoviruses, HumanAdenovirus Infections, HumanCapsid ProteinsCell LineCysteine EndopeptidasesHumansViral ProteinsVirionCapsid ProteinsCysteine EndopeptidasesL3 23K protein, adenovirusViral Proteins

Identifiers

PMID24227847
PMCPMC3911601
OpenAlexW1984099308

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.