Evidence map›Paper›PMID 19007407›Full record

ArticleMolecular microbiology2009

The Fusobacterium nucleatum outer membrane protein RadD is an arginine-inhibitable adhesin required for inter-species adherence and the structured architecture of multispecies biofilm.

Christopher W Kaplan, Renate Lux, Susan Kinder Haake, Wenyuan Shi

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

161 citing papers in PubMed, 251 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
    Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. RadD fromeLife · 2026
    Article
  7. Review
  8. Pathogenic Roles ofPathogens (Basel, Switzerland) · 2026
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. CLASI-FISH Imaging of Fusobacterium in Oral Microbial Communities.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  14. Article
  15. Frontiers in cellular and infection microbiology · 2026
    Review
  16. Gene Silencing by CRISPR Interference in Fusobacterium nucleatum.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  17. Review
  18. Article
  19. Gut microbes · 2025
    Article
  20. Article

101 more citing papers are in PubMed but not listed here.

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.

Christopher W KaplanSchool of Dentistry, UCLA, Los Angeles, CA, USA.
Renate Lux
Susan Kinder Haake
Wenyuan Shi
University of California, Los Angeles · US

Funding

Genetic Systems for Fusobacterium nucleatumR01DE015348 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HAAKE, SUSAN KINDER · 2005 to 2008
$1.1M
NIDCR NIH HHS DE015348NIDCR NIH HHS R01 DE015348
6 · The paper itself

Abstract

A defining characteristic of the suspected periodontal pathogen Fusobacterium nucleatum is its ability to adhere to a plethora of oral bacteria. This distinguishing feature is suggested to play an important role in oral biofilm formation and pathogenesis, with fusobacteria proposed to serve as central 'bridging organisms' in the architecture of the oral biofilm bringing together species which would not interact otherwise. Previous studies indicate that these bacterial interactions are mediated by galactose- or arginine-inhibitable adhesins although genetic evidence for the role and nature of these proposed adhesins remains elusive. To characterize these adhesins at the molecular level, the genetically transformable F. nucleatum strain ATCC 23726 was screened for adherence properties, and arginine-inhibitable adhesion was evident, while galactose-inhibitable adhesion was not detected. Six potential arginine-binding proteins were isolated from the membrane fraction of F. nucleatum ATCC 23726 and identified via mass spectroscopy as members of the outer membrane family of proteins in F. nucleatum. Inactivation of the genes encoding these six candidates for arginine-inhibitable adhesion and two additional homologues revealed that only a mutant derivative carrying an insertion in Fn1526 (now designated as radD) demonstrated significantly decreased co-aggregation with representatives of the gram-positive 'early oral colonizers'. Lack of the 350 kDa outer membrane protein encoded by radD resulted in the failure to form the extensive structured biofilm observed with the parent strain when grown in the presence of Streptococcus sanguinis ATCC 10556. These findings indicate that radD is responsible for arginine-inhibitable adherence of F. nucleatum and provides definitive molecular evidence that F. nucleatum adhesins play a vital role in inter-species adherence and multispecies biofilm formation.

Indexed as

Bacterial AdhesionBiofilmsAdhesins, BacterialArginineFusobacterium nucleatumGene SilencingMutagenesisOperonRNA, BacterialSpecies SpecificityStreptococcus sanguisAdhesins, BacterialArginineRNA, Bacterial

Identifiers

PMID19007407
PMCPMC2741168
OpenAlexW2005421221

What OpenQuestion holds

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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.