Evidence map›Paper›PMID 21696465›Full record

ArticleMolecular microbiology2011

Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development.

Arunima Mishra, Bharanidharan Devarajan, Melissa E Reardon, Prabhat Dwivedi, Vengadesan Krishnan, John O Cisar, Asis Das, Sthanam V L Narayana, Hung Ton-That

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Enigmatic Pilus-Like Endospore Appendages ofInternational journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Cell-to-cell interaction requires optimal positioning of a pilus tip adhesin modulated by gram-positive transpeptidase enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Genetics ofMicrobiology spectrum · 2019
    Article
  12. Molecular strategy for blocking isopeptide bond formation in nascent pilin proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.International journal of molecular sciences · 2017
    Review
  19. Article
  20. 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

9 authors at 3 institutions in 1 country.

Arunima MishraDepartment of Microbiology & Molecular Genetics, University of Texas Health Science Center, Houston, TX, USA.
Bharanidharan Devarajan
Melissa E Reardon
Prabhat Dwivedi
Vengadesan Krishnan
John O Cisar
Asis Das
Sthanam V L Narayana
Hung Ton-That
The University of Texas Health Science Center at Houston · USNational Institute of Dental and Craniofacial Research · USUConn Health · US

Funding

Molecular Biology of Oral Microbial Adhesins and ReceptorsZIADE000672 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI CISAR, JOHN O · 2009 to 2016
$6.9M
Molecular Assembly on the Cell Surface of ActinomycesR01DE017382 · NIDCR · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI Hung Ton-That · 2008 to 2026
$6.7M
Mechanism of Cell Surface Assembly Catalyzed by SortasesR01AI073521 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STHANAM, NARAYANA VL · 2008 to 2012
$1.8M
Characterization of Complement C3-convertasesR01AI064815 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STHANAM, NARAYANA VL · 2005 to 2009
$1.6M
NIAID NIH HHS AI064815NIAID NIH HHS R01 AI064815NIAID NIH HHS R01 AI073521NIDCR NIH HHS DE017382NIDCR NIH HHS R01 DE017382
6 · The paper itself

Abstract

By combining X-ray crystallography and modelling, we describe here the atomic structure of distinct adhesive moieties of FimA, the shaft fimbrillin of Actinomyces type 2 fimbriae, which uniquely mediates the receptor-dependent intercellular interactions between Actinomyces and oral streptococci as well as host cells during the development of oral biofilms. The FimA adhesin is built with three IgG-like domains, each of which harbours an intramolecular isopeptide bond, previously described in several Gram-positive pilins. Genetic and biochemical studies demonstrate that although these isopeptide bonds are dispensable for fimbrial assembly, cell-cell interactions and biofilm formation, they contribute significantly to the proteolytic stability of FimA. Remarkably, FimA harbours two autonomous adhesive modules, which structurally resemble the Staphylococcus aureus Cna B domain. Each isolated module can bind the plasma glycoprotein asialofetuin as well as the polysaccharide receptors present on the surface of oral streptococci and epithelial cells. Thus, FimA should serve as an excellent paradigm for the development of therapeutic strategies and elucidating the precise molecular mechanisms underlying the interactions between cellular receptors and Gram-positive fimbriae.

Indexed as

ActinomycesAdhesins, BacterialAmino Acid SequenceAsialoglycoproteinsBacterial AdhesionBiofilmsCrystallography, X-RayFetuinsFimbriae, BacterialFimbriae ProteinsImmunoglobulin GReceptors, Cell SurfaceSequence AlignmentStreptococcus oralisStreptococcus pneumoniaeToothAdhesins, BacterialasialofetuinAsialoglycoproteinsFetuinsFimbriae ProteinsImmunoglobulin GReceptors, Cell Surface

Identifiers

PMID21696465
PMCPMC3177855
OpenAlexW2125967313

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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.