Evidence map›Paper›PMID 14996807›Full record

ArticleJournal of bacteriology2004

Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology.

Christoph Mader, Carina Huber, Dieter Moll, Uwe B Sleytr, Margit Sára

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Adaptation of the binding domain ofFrontiers in microbiology · 2023
    Article
  5. Article
  6. Article
  7. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  8. Review
  9. Biogenesis and functions of bacterial S-layers.Nature reviews. Microbiology · 2014
    Review
  10. Article
  11. Article
  12. S-layer protein self-assembly.International journal of molecular sciences · 2013
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Composite S-layer lipid structures.Journal of structural biology · 2009
    Review
  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

5 authors at 2 institutions in 1 country.

Christoph MaderCenter for Ultrastructure Research and Ludwig Boltzmann Institute for Molecular Nanotechnology, University of Natural Resources and Applied Life Sciences Vienna, Austria. Christoph.mader@gmx.net
Carina Huber
Dieter Moll
Uwe B Sleytr
Margit Sára
BOKU University · ATLudwig Boltzmann Institute for Digital Health and Prevention

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction between S-layer protein SbsB and the secondary cell wall polymer (SCWP) of Geobacillus stearothermophilus PV72/p2 was investigated by real-time surface plasmon resonance biosensor technology. The SCWP is an acidic polysaccharide that contains N-acetylglucosamine, N-acetylmannosamine, and pyruvic acid. For interaction studies, recombinant SbsB (rSbsB) and two truncated forms consisting of either the S-layer-like homology (SLH) domain (3SLH) or the residual part of SbsB were used. Independent of the setup, the data showed that the SLH domain was exclusively responsible for SCWP binding. The interaction was found to be highly specific, since neither the peptidoglycan nor SCWPs from other organisms nor other polysaccharides were recognized. Data analysis from that setup in which 3SLH was immobilized on a sensor chip and SCWP represented the soluble analyte was done in accordance with a model that describes binding of a bivalent analyte to a fixed ligand in terms of an overall affinity for all binding sites. The measured data revealed the presence of at least two binding sites on a single SCWP molecule with a distance of about 14 nm and an overall Kd of 7.7 x 10(-7) M. Analysis of data from the inverted setup in which the SCWP was immobilized on a sensor chip was done in accordance with an extension of the heterogeneous-ligand model, which indicated the existence of three binding sites with low (Kd = 2.6 x 10(-5) M), medium (Kd = 6.1 x 10(-8) M), and high (Kd = 6.7 x 10(-11) M) affinities. Since in this setup 3SLH was the soluble analyte and the presence of small amounts of oligomers in even monomeric protein solutions cannot be excluded, the high-affinity binding site may result from avidity effects caused by binding of at least dimeric 3SLH. Solution competition assays performed with both setups confirmed the specificity of the protein-carbohydrate interaction investigated.

Indexed as

Bacterial ProteinsBinding SitesBiopolymersCell WallCrystallizationGeobacillus stearothermophilusMembrane ProteinsPolysaccharides, BacterialSurface Plasmon ResonanceBacterial ProteinsBiopolymersMembrane ProteinsPolysaccharides, BacterialSbsB protein, Bacillus stearothermophilus

Identifiers

PMID14996807
PMCPMC355981
OpenAlexW2111797318

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.