Evidence map›Paper›PMID 26576675›Full record

ArticleBMC biotechnology2015

Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS.

Thomas McDonnell, Charis Pericleous, Emmanuelle Laurine, Rita Tommasi, Acely Garza-Garcia, Ian Giles, Yiannis Ioannou, Anisur Rahman

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

8 authors.

Thomas McDonnellCentre for Rheumatology, Division of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JF, UK. Thomas.mcdonnell.11@ucl.ac.uk.
Charis PericleousCentre for Rheumatology, Division of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JF, UK. c.pericleous@ucl.ac.uk.
Emmanuelle LaurinePolyTherics, Babraham Research Campus, Babraham, CB22 3AT, Cambridge, UK. elaurine@hotmail.com.
Rita TommasiPolyTherics, Babraham Research Campus, Babraham, CB22 3AT, Cambridge, UK. Rita.Tommasi@gmail.com.
Acely Garza-GarciaStructural Biology, Medical Research Council National Institute for Medical Research, London, UK. acely.garza@crick.ac.uk.
Ian GilesCentre for Rheumatology, Division of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JF, UK. i.giles@ucl.ac.uk.
Yiannis IoannouCentre for Rheumatology, Division of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JF, UK. y.ioannou@ucl.ac.uk.
Anisur RahmanCentre for Rheumatology, Division of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JF, UK. Anisur.rahman@ucl.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn this paper we describe a novel method to achieve high yield bacterial expression of a small protein domain with considerable therapeutic potential; Domain I of Beta-2-glycoprotein I (β2GPI). β2GPI is intrinsic to the pathological progression of the Antiphospholipid Syndrome (APS). Patients develop autoantibodies targeting an epitope located on the N-terminal Domain I of β2GPI rendering this domain of interest as a possible therapeutic.

resultsThis new method of production of Domain I of β2GPI has increased the production yield by ~20 fold compared to previous methods in E.coli. This largely scalable, partially automated method produces 50-75 mg of pure, folded, active Domain I of β2GPI per litre of expression media.

conclusionThe application of this method may enable production of Domain I on sufficient scale to allow its use as a therapeutic.

Indexed as

AdultAntiphospholipid SyndromeAutomation, Laboratorybeta 2-Glycoprotein IEscherichia coliFemaleHumansInclusion BodiesMaleMiddle AgedProtein Structure, TertiaryRecombinant Fusion Proteinsbeta 2-Glycoprotein IRecombinant Fusion Proteins

Identifiers

PMID26576675
PMCPMC4650279

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.