Evidence map›Paper›PMID 19661180›Full record

ArticleMicrobiology (Reading, England)2009

Multiple adhesin proteins on the cell surface of Streptococcus gordonii are involved in adhesion to human fibronectin.

Nicholas S Jakubovics, Jane L Brittan, Lindsay C Dutton, Howard F Jenkinson

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. The structure ofInfection and immunity · 2026
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  13. Serine-Rich Repeat Adhesins Contribute toFrontiers in microbiology · 2017
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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

4 authors at 3 institutions in 1 country.

Nicholas S JakubovicsSchool of Dental Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4BW, UK.
Jane L BrittanDepartment of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
Lindsay C DuttonDepartment of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
Howard F JenkinsonDepartment of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
University of Bristol · GBNewcastle University · GBUniversity Of Bristol Dental Hospital · GB

Funding

Wellcome TrustWellcome Trust 064832
6 · The paper itself

Abstract

Adhesion of bacterial cells to fibronectin (FN) is thought to be a pivotal step in the pathogenesis of invasive infectious diseases. Viridans group streptococci such as Streptococcus gordonii are considered commensal members of the oral microflora, but are important pathogens in infective endocarditis. S. gordonii expresses a battery of cell-surface adhesins that act alone or in concert to bind host receptors. Here, we employed molecular genetic approaches to determine the relative contributions of five known S. gordonii surface proteins to adherence to human FN. Binding levels to FN by isogenic mutants lacking Hsa glycoprotein were reduced by 70 %, while mutants lacking CshA and CshB fibrillar proteins showed approximately 30 % reduced binding. By contrast, disruption of antigen I/II adhesin genes sspA and sspB in a wild-type background did not result in reduced FN binding. Enzymic removal of sialic acids from FN led to reduced S. gordonii DL1 adhesion (>50 %), but did not affect binding by the hsa mutant, indicating that Hsa interacts with sialic acid moieties on FN. Conversely, desialylation of FN did not affect adherence levels of Lactococcus lactis cells expressing SspA or SspB polypeptides. Complementation of the hsa mutant partially restored adhesion to FN. A model is proposed for FN binding by S. gordonii in which Hsa and CshA/CshB are primary adhesins, and SspA or SspB play secondary roles. Understanding the basis of oral streptococcal interactions with FN will provide a foundation for development of new strategies to control infective endocarditis.

Indexed as

Bacterial AdhesionAdhesins, Bacterialalpha-FetoproteinsBacterial ProteinsCarrier ProteinsFibronectinsGenetic Complementation TestHemagglutinins, ViralHumansMembrane ProteinsSialic AcidsStreptococcus gordoniiAdhesins, Bacterialalpha-FetoproteinsBacterial ProteinsCarrier ProteinsCshA protein, Streptococcus gordoniiFibronectinsHemagglutinins, Viralhsa protein, Streptococcus gordoniiMembrane ProteinsSialic AcidsSspA protein, bacteria

Identifiers

PMID19661180
PMCPMC2885655
OpenAlexW2037895543

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.