Evidence map›Paper›PMID 28256592›Full record

ArticleScientific reports2017

Yield Optimisation of Hepatitis B Virus Core Particles in E. coli Expression System for Drug Delivery Applications.

Izzat Fahimuddin Bin Mohamed Suffian, Mitla Garcia-Maya, Paul Brown, Tam Bui, Yuya Nishimura, Amir Rafiq Bin Mohammad Johari Palermo, Chiaki Ogino, Akihiko Kondo, Khuloud T Al-Jamal

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
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  4. 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

9 authors.

Izzat Fahimuddin Bin Mohamed SuffianInstitute of Pharmaceutical Science, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, UK.
Mitla Garcia-MayaRandall Division of Cell &Molecular Biophysics, King's College London, New Hunt's House, London SE1 1UL, UK.
Paul BrownRandall Division of Cell &Molecular Biophysics, King's College London, New Hunt's House, London SE1 1UL, UK.
Tam BuiBiomolecular Spectroscopy Centre, King's College London, The Wolfson Wing, Hodgkin Building, SE1 1UL, UK.
Yuya NishimuraDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
Amir Rafiq Bin Mohammad Johari PalermoBarts and The London School of Medicine and Dentistry, Queen Mary University of London, 4 Newark Street, London E1 2AT, UK.
Chiaki OginoDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
Akihiko KondoDepartment of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
Khuloud T Al-JamalInstitute of Pharmaceutical Science, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/J008656/1
6 · The paper itself

Abstract

An E. coli expression system offers a mean for rapid, high yield and economical production of Hepatitis B Virus core (HBc) particles. However, high-level production of HBc particles in bacteria is demanding and optimisation of HBc particle yield from E. coli is required to improve laboratory-scale productivity for further drug delivery applications. Production steps involve bacterial culture, protein isolation, denaturation, purification and finally protein assembly. In this study, we describe a modified E. coli based method for purifying HBc particles and compare the results with those obtained using a conventional purification method. HBc particle morphology was confirmed by Atomic Force Microscopy (AFM). Protein specificity and secondary structure were confirmed by Western Blot and Circular Dichroism (CD), respectively. The modified method produced ~3-fold higher yield and greater purity of wild type HBc particles than the conventional method. Our results demonstrated that the modified method produce a better yield and purity of HBc particles in an E. coli-expression system, which are fully characterised and suitable to be used for drug delivery applications.

Indexed as

Blotting, WesternCircular DichroismDrug CarriersEscherichia coliGene ExpressionHepatitis B Core AntigensHepatitis B virusMicroscopy, Atomic ForceProtein ConformationRecombinant ProteinsVirionDrug CarriersHepatitis B Core AntigensRecombinant Proteins

Identifiers

PMID28256592
PMCPMC5335696

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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.