Evidence map›Paper›PMID 21821042›Full record

ArticleJournal of molecular biology2011

The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination.

Altaira D Dearborn, Michael S Spilman, Priyadarshan K Damle, Jenny R Chang, Eric B Monroe, Jamil S Saad, Gail E Christie, Terje Dokland

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Formation and role of the portal ofbioRxiv : the preprint server for biology · 2026
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  6. Structure and host specificity ofScience advances · 2022
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  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Convergent evolution of pathogenicity islands in helper cos phage interference.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

8 authors at 2 institutions in 1 country.

Altaira D DearbornDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Michael S Spilman
Priyadarshan K Damle
Jenny R Chang
Eric B Monroe
Jamil S Saad
Gail E Christie
Terje Dokland
University of Alabama at Birmingham · USVirginia Commonwealth University · US

Funding

Structural basis for pathogenicity island mobilization in S. aureusR01AI083255 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DOKLAND, TERJE · 2009 to 2023
$5.6M
Helper Phage Mobilization of Staphylococcal Enterotoxin GenesR21AI067654 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CHRISTIE, GAIL E · 2006 to 2007
$399k
Helper phage mobilization of S. aureus superantigen pathogenicity islandsR56AI081837 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CHRISTIE, GAIL E · 2010 to 2010
$372k
Structure and size determination of S. aureus pathogenicity island capsidsR21AI071982 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DOKLAND, TERJE · 2007 to 2008
$372k
Studying HIV gp120 Glycosylation with Mass SpectrometryF32GM087994 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MONROE, ERIC B · 2009 to 2011
$135k
NIAID NIH HHS R01 AI083255NIAID NIH HHS R21 AI067654NIAID NIH HHS R21 AI071982NIAID NIH HHS R56 AI081837NIGMS NIH HHS F32 GM087994
6 · The paper itself

Abstract

Staphylococcus aureus pathogenicity island 1 (SaPI1) is a mobile genetic element that carries genes for several superantigen toxins. SaPI1 is normally stably integrated into the host genome but can become mobilized by "helper" bacteriophage 80α, leading to the packaging of SaPI1 genomes into phage-like transducing particles that are composed of structural proteins supplied by the helper phage but having smaller capsids. We show that the SaPI1-encoded protein gp6 is necessary for efficient formation of small capsids. The NMR structure of gp6 reveals a dimeric protein with a helix-loop-helix motif similar to that of bacteriophage scaffolding proteins. The gp6 dimer matches internal densities that bridge capsid subunits in cryo-electron microscopy reconstructions of SaPI1 procapsids, suggesting that gp6 acts as an internal scaffolding protein in capsid size determination.

Indexed as

Amino Acid SequenceCapsidCapsid ProteinsComputer SimulationGenomic IslandsModels, BiologicalModels, MolecularOrganelle SizeOrganisms, Genetically ModifiedProtein FoldingProtein MultimerizationProtein Structure, QuaternaryStaphylococcus aureusVirus AssemblyCapsid Proteins

Identifiers

PMID21821042
PMCPMC3175317
OpenAlexW2089240975

What OpenQuestion holds

Textmetadata
LicenceTDM
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.