Evidence map›Paper›PMID 15006773›Full record

ArticleApplied and environmental microbiology2004

Construction of a functional S-layer fusion protein comprising an immunoglobulin G-binding domain for development of specific adsorbents for extracorporeal blood purification.

Christine Völlenkle, Stefan Weigert, Nicola Ilk, Eva Egelseer, Viktoria Weber, Fritz Loth, Dieter Falkenhagen, Uwe B Sleytr, Margit Sára

Open access · greenAbstract readComparative Study
In one paragraph

Article in Applied and environmental microbiology, 2004. 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
9.5field-weighted citation impact, top 2% 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, 109 citations in OpenAlex.

  1. Article
  2. Article
  3. Electrochemical Biosensors Based on S-Layer Proteins.Sensors (Basel, Switzerland) · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  11. S-layer protein self-assembly.International journal of molecular sciences · 2013
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Immunoabsorbent nanoparticles based on a tobamovirus displaying protein A.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  19. Article
  20. Recent advances of protein microarrays.Current opinion in chemical biology · 2006
    Review
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 2 countries.

Christine VöllenkleCenter for Ultrastructure Research and Ludwig Boltzmann Institute for Molecular Nanotechnology, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Stefan Weigert
Nicola Ilk
Eva Egelseer
Viktoria Weber
Fritz Loth
Dieter Falkenhagen
Uwe B Sleytr
Margit Sára
Ludwig Boltzmann Institute for Digital Health and PreventionUniversität für Weiterbildung Krems · ATFraunhofer Institute for Applied Polymer Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chimeric gene encoding a C-terminally-truncated form of the S-layer protein SbpA from Bacillus sphaericus CCM 2177 and two copies of the Fc-binding Z-domain was constructed, cloned, and heterologously expressed in Escherichia coli HMS174(DE3). The Z-domain is a synthetic analogue of the B-domain of protein A, capable of binding the Fc part of immunoglobulin G (IgG). The S-layer fusion protein rSbpA(31-1068)/ZZ retained the specific properties of the S-layer protein moiety to self-assemble in suspension and to recrystallize on supports precoated with secondary cell wall polymer (SCWP), which is the natural anchoring molecule for the S-layer protein in the bacterial cell wall. Due to the construction principle of the S-layer fusion protein, the ZZ-domains remained exposed on the outermost surface of the protein lattice. The binding capacity of the native or cross-linked monolayer for human IgG was determined by surface plasmon resonance measurements. For batch adsorption experiments, 3-microm-diameter, biocompatible cellulose-based, SCWP-coated microbeads were used for recrystallization of the S-layer fusion protein. In the case of the native monolayer, the binding capacity for human IgG was 5.1 ng/mm(2), whereas after cross-linking with dimethyl pimelimidate, 4.4 ng of IgG/mm(2) was bound. This corresponded to 78 and 65% of the theoretical saturation capacity of a planar surface for IgGs aligned in the upright position, respectively. Compared to commercial particles used as immunoadsorbents to remove autoantibodies from sera of patients suffering from an autoimmune disease, the IgG binding capacity of the S-layer fusion protein-coated microbeads was at least 20 times higher. For that reason, this novel type of microbeads should find application in the microsphere-based detoxification system.

Indexed as

Autoimmune DiseasesBacterial ProteinsBase SequenceBinding SitesCloning, MolecularCrystallizationDNA, RecombinantHumansImmunoglobulin GImmunosorbentsIn Vitro TechniquesMembrane GlycoproteinsMicroscopy, Atomic ForceMicroscopy, ElectronMicrospheresProtein Structure, TertiaryBacterial ProteinsDNA, RecombinantImmunoglobulin GImmunosorbentsMembrane GlycoproteinsRecombinant Fusion ProteinsS-layer proteins

Identifiers

PMID15006773
PMCPMC368406
OpenAlexW2159449648

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.