Evidence map›Paper›PMID 11544229›Full record

ArticleJournal of bacteriology2001

Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance.

C M Waters, G M Dunny

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

33 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Article
  3. Insights into ecology, pathogenesis, and biofilm formation ofMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Enterococcal Genetics.Microbiology spectrum · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Biological diversity of prokaryotic type IV secretion systems.Microbiology and molecular biology reviews : MMBR · 2009
    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

2 authors at 1 institution in 1 country.

C M WatersDepartment of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA.
G M Dunny
University of Minnesota Medical Center · US

Funding

GENETIC FUNCTIONS OF CONJUGATIVE STREPTOCOCCAL R FACTORR01GM049530 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DUNNY, GARY M · 1992 to 2014
$3.6M
ROLE OF CELLWALL COMPONENTS IN ENTEROCOCCAL ENDOCARDITISR01HL051987 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DUNNY, GARY M · 1995 to 2006
$2.1M
MOLECULAR MECHANISMS OF INFECTIOUS DISEASE TRAININGT32AI007421 · NIAID · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HAASE, ASHLEY T. · 1995 to 2004
$1.2M
NHLBI NIH HHS HL-51987NHLBI NIH HHS R01 HL051987NIAID NIH HHS 5 T32 AI07421-5NIAID NIH HHS T32 AI007421NIGMS NIH HHS GM-49530NIGMS NIH HHS R01 GM049530
6 · The paper itself

Abstract

Pheromone-inducible aggregation substance (AS) proteins of Enterococcus faecalis are essential for high-efficiency conjugation of the sex pheromone plasmids and also serve as virulence factors during host infection. A number of different functions have been attributed to AS in addition to bacterial cell aggregation, including adhesion to host cells, adhesion to fibrin, increased cell surface hydrophobicity, resistance to killing by polymorphonuclear leukocytes and macrophages, and increased vegetation size in an experimental endocarditis model. Relatively little information is available regarding the structure-activity relationship of AS. To identify functional domains, a library of 23 nonpolar 31-amino-acid insertions was constructed in Asc10, the AS encoded by the plasmid pCF10, using the transposons TnlacZ/in and TnphoA/in. Analysis of these insertions revealed a domain necessary for donor-recipient aggregation that extends further into the amino terminus of the protein than previously reported. In addition, insertions in the C terminus of the protein also reduced aggregation. As expected, the ability to aggregate correlates with efficient plasmid transfer. The results also indicated that an increase in cell surface hydrophobicity resulting from AS expression is not sufficient to mediate bacterial aggregation.

Indexed as

Bacterial AdhesionBacterial ProteinsDNA Transposable ElementsEnterococcus faecalisFlow CytometryMutagenesis, InsertionalPheromonesPlasmidsSpectrophotometryStructure-Activity RelationshipSurface PropertiesTemperatureaggregation substance, Enterococcus faecalisBacterial ProteinsDNA Transposable ElementsPheromones

Identifiers

PMID11544229
PMCPMC95458
OpenAlexW2009326408

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.