Evidence map›Paper›PMID 12089001›Full record

ArticleApplied and environmental microbiology2002

Molecular characterization of the S-layer gene, sbpA, of Bacillus sphaericus CCM 2177 and production of a functional S-layer fusion protein with the ability to recrystallize in a defined orientation while presenting the fused allergen.

Nicola Ilk, Christine Völlenkle, Eva M Egelseer, Andreas Breitwieser, Uwe B Sleytr, Margit Sára

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 126 citations in OpenAlex.

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  12. Article
  13. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  14. S-layer protein self-assembly.International journal of molecular sciences · 2013
    Article
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  16. 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

6 authors at 1 institution.

Nicola IlkCenter for Ultrastructure Research, Ludwig Boltzmann-Institute for Molecular Nanotechnology, University of Agricultural Sciences, Gregor Mendelstrasse 33, 1180 Vienna, Austria.
Christine Völlenkle
Eva M Egelseer
Andreas Breitwieser
Uwe B Sleytr
Margit Sára
Ludwig Boltzmann Institute for Digital Health and Prevention

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nucleotide sequence encoding the crystalline bacterial cell surface (S-layer) protein SbpA of Bacillus sphaericus CCM 2177 was determined by a PCR-based technique using four overlapping fragments. The entire sbpA sequence indicated one open reading frame of 3,804 bp encoding a protein of 1,268 amino acids with a theoretical molecular mass of 132,062 Da and a calculated isoelectric point of 4.69. The N-terminal part of SbpA, which is involved in anchoring the S-layer subunits via a distinct type of secondary cell wall polymer to the rigid cell wall layer, comprises three S-layer-homologous motifs. For screening of amino acid positions located on the outer surface of the square S-layer lattice, the sequence encoding Strep-tag I, showing affinity to streptavidin, was linked to the 5' end of the sequence encoding the recombinant S-layer protein (rSbpA) or a C-terminally truncated form (rSbpA(31-1068)). The deletion of 200 C-terminal amino acids did not interfere with the self-assembly properties of the S-layer protein but significantly increased the accessibility of Strep-tag I. Thus, the sequence encoding the major birch pollen allergen (Bet v1) was fused via a short linker to the sequence encoding the C-terminally truncated form rSpbA(31-1068). Labeling of the square S-layer lattice formed by recrystallization of rSbpA(31-1068)/Bet v1 on peptidoglycan-containing sacculi with a Bet v1-specific monoclonal mouse antibody demonstrated the functionality of the fused protein sequence and its location on the outer surface of the S-layer lattice. The specific interactions between the N-terminal part of SbpA and the secondary cell wall polymer will be exploited for an oriented binding of the S-layer fusion protein on solid supports to generate regularly structured functional protein lattices.

Indexed as

BacillusBacterial ProteinsCloning, MolecularCopperCrystallizationEscherichia coliGene ExpressionImmunohistochemistryMembrane GlycoproteinsMonosaccharide Transport ProteinsPeptide FragmentsPolylysineRecombinant Fusion ProteinsBacterial ProteinsCopperMembrane GlycoproteinsMonosaccharide Transport ProteinsPeptide FragmentsPolylysineRecombinant Fusion ProteinsSbpA protein, bacteriaS-layer proteins

Identifiers

PMID12089001
PMCPMC126809
OpenAlexW2086115755

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.