Evidence map›Paper›PMID 37036352›Full record

ArticleMicrobiology spectrum2023

Efficient Autotransporter-Mediated Extracellular Secretion of a Heterologous Recombinant Protein by Escherichia coli.

Irene Beriotto, Christopher Icke, Yanina R Sevastsyanovich, Amanda E Rossiter, Giacomo Romagnoli, Silvana Savino, Freya J Hodges, Jeffrey A Cole, Allan Saul, Calman A MacLennan and 3 more

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2023. 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
1.2field-weighted citation impact, top 21% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  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

13 authors at 4 institutions in 3 countries.

Irene BeriottoInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.
Christopher IckeInstitute for Molecular Bioscience, University of Queensland, Brisbane, Queensland, Australia.
Yanina R SevastsyanovichInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.
Amanda E RossiterInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.
Giacomo RomagnoliGSK Vaccines Institute for Global Health Srl, Siena, Italy.
Silvana SavinoGSK Vaccines Institute for Global Health Srl, Siena, Italy.
Freya J HodgesInstitute for Molecular Bioscience, University of Queensland, Brisbane, Queensland, Australia.
Jeffrey A ColeInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.
Allan SaulGSK Vaccines Institute for Global Health Srl, Siena, Italy.
Calman A MacLennanGSK Vaccines Institute for Global Health Srl, Siena, Italy.
Adam F CunninghamInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.ORCID 0000-0003-0248-964X
Francesca MicoliGSK Vaccines Institute for Global Health Srl, Siena, Italy.
Ian R HendersonInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United Kingdom.ORCID 0000-0002-9954-4977
Toscana Life Sciences · ITUniversity of Birmingham · GBThe University of Queensland · AUUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The autotransporter protein secretion system has been used previously to target the secretion of heterologous proteins to the bacterial cell surface and the extracellular milieu at the laboratory scale. The platform is of particular interest for the production of "difficult" recombinant proteins that might cause toxic effects when produced intracellularly. One such protein is IrmA. IrmA is a vaccine candidate that is produced in inclusion bodies requiring refolding. Here, we describe the use and scale-up of the autotransporter system for the secretion of an industrially relevant protein (IrmA). A plasmid expressing IrmA was constructed such that the autotransporter platform could secrete IrmA into the culture supernatant fraction. The autotransporter platform was suitable for the production and purification of IrmA with comparable physical properties to the protein produced in the cytoplasm. The production of IrmA was translated to scale-up protein production conditions resulting in a yield of 29.3 mg/L of IrmA from the culture supernatant, which is consistent with yields of current industrial processes.

Indexed as

Escherichia coliEscherichia coli ProteinsCell MembraneRecombinant ProteinsType V Secretion SystemsEscherichia coli ProteinsRecombinant ProteinsType V Secretion Systemsautotransporterautotransporter proteinsEscherichia coliinclusion bodiesPet autotransporter platformprotein secretionrecombinant protein productionsecretion

Identifiers

PMID37036352
PMCPMC10269718
OpenAlexW4363645912

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.