Evidence map›Paper›PMID 19383683›Full record

ArticleMicrobiology (Reading, England)2009

Identification of novel LPXTG-linked surface proteins from Streptococcus gordonii.

Julia R Davies, Gunnel Svensäter, Mark C Herzberg

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  6. Review
  7. Proteomic response inJournal of oral microbiology · 2021
    Article
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  9. Microorganisms · 2020
    Review
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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

3 authors at 2 institutions in 2 countries.

Julia R DaviesDepartment of Oral Biology, Faculty of Odontology, Malmö University, Carl Gustavs väg 34, Malmö S-20506, Sweden.
Gunnel SvensäterDepartment of Oral Biology, Faculty of Odontology, Malmö University, Carl Gustavs väg 34, Malmö S-20506, Sweden.
Mark C HerzbergMucosal and Vaccine Research Center, Minneapolis VA Medical Center, Minneapolis, MN 55417, USA.
Malmö University · SEMinneapolis VA Medical Center · US

Funding

S. SANGUIS ADHESION--MOLECULAR BASIS OF SPECIFICITYR01DE008590 · NIDCR · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HERZBERG, MARK C · 1990 to 2009
$3.7M
Biotechnology and Biological Sciences Research CouncilNIDCR NIH HHS R01 DE008590NIDCR NIH HHS R01DE08590
6 · The paper itself

Abstract

Surface adhesion plays an essential part in the survival of the commensal organism Streptococcus gordonii in the oral cavity as well as during opportunistic infections such as endocarditis. At least two types of cell surface protein involved in adhesion are found on the surface of Gram-positive bacteria: those anchored via an LPXTG motif by the enzyme sortase A (SrtA) and those associated with the cell surface by, as yet, unknown mechanisms. In srtA(-) mutants, LPXTG-containing proteins have been shown to be released rather than cross-linked to the cell wall. We have therefore used 2D gel electrophoresis of released proteins from an srtA(-) mutant as well as the wild-type strain, followed by peptide identification by MS, to identify a set of novel proteins predicted to be present on the surface of S. gordonii DL1. This includes two large LPXTG-linked proteins (SGO_0707 and SGO_1487), which both contain tandemly repeated sequences similar to those present in known fibrillar adhesins. A 5'-nucleotidase and a protein with a putative collagen-binding domain, both containing LPXTG motifs, were also identified. Anchorless proteins with known chaperone, stress response and elongation factor functions, apparently responsible for bacterial binding to keratinocytes and saliva-coated surfaces in the absence of the LPXTG-linked adhesins, were also associated with the cell surface. These data reveal a range of proteins to be present on the S. gordonii DL1 cell surface, the expression of which plays an important role in adhesion to epithelia and which represent likely candidates for novel virulence factors in S. gordonii.

Indexed as

Streptococcus gordoniiAmino Acid MotifsAminoacyltransferasesBacterial AdhesionBacterial Outer Membrane ProteinsBacterial ProteinsCysteine EndopeptidasesDental PlaqueElectrophoresis, Gel, Two-DimensionalHumansKeratinocytesMouthSalivaStreptococcal InfectionsVirulenceAminoacyltransferasesBacterial Outer Membrane ProteinsBacterial ProteinsCysteine Endopeptidasessortase A

Identifiers

PMID19383683
PMCPMC2888288
OpenAlexW2090193533

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.