Evidence map›Paper›PMID 31887188›Full record

ArticlePloS one2019

A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.

Márk Somogyi, Tamás Szimler, Attila Baksa, Barbara M Végh, Tamás Bakos, Katalin Paréj, Csaba Ádám, Áron Zsigmond, Márton Megyeri, Beáta Flachner and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

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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

15 authors at 1 institution in 1 country.

Márk SomogyiInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Tamás SzimlerInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Attila BaksaInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Barbara M VéghInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Tamás BakosInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Katalin ParéjInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Csaba ÁdámInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Áron ZsigmondInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Márton MegyeriInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Beáta FlachnerInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Ráchel SajóInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Éva GráczerInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.ORCID 0000-0002-8312-5591
Péter ZávodszkyInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
István HajdúInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.ORCID 0000-0003-2312-0833
László BeinrohrInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pázmány Péter sétány, Budapest, Hungary.
Institute of Molecular Life Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have developed a unified, versatile vector set for expression of recombinant proteins, fit for use in any bacterial, yeast, insect or mammalian cell host. The advantage of this system is its versatility at the vector level, achieved by the introduction of a novel expression cassette. This cassette contains a unified multi-cloning site, affinity tags, protease cleavable linkers, an optional secretion signal, and common restriction endonuclease sites at key positions. This way, genes of interest and all elements of the cassette can be switched freely among the vectors, using restriction digestion and ligation without the need of polymerase chain reaction (PCR). This vector set allows rapid protein expression screening of various hosts and affinity tags. The reason behind this approach was that it is difficult to predict which expression host and which affinity tag will lead to functional expression. The new system is based on four optimized and frequently used expression systems (Escherichia coli pET, the yeast Pichia pastoris, pVL and pIEx for Spodoptera frugiperda insect cells and pLEXm based mammalian systems), which were modified as described above. The resulting vector set was named pONE series. We have successfully applied the pONE vector set for expression of the following human proteins: the tumour suppressor RASSF1A and the protein kinases Aurora A and LIMK1. Finally, we used it to express the large multidomain protein, Rho-associated protein kinase 2 (ROCK2, 164 kDa) and demonstrated that the yeast Pichia pastoris reproducibly expresses the large ROCK2 kinase with identical activity to the insect cell produced counterpart. To our knowledge this is among the largest proteins ever expressed in yeast. This demonstrates that the cost-effective yeast system can match and replace the industry-standard insect cell expression system even for large and complex mammalian proteins. These experiments demonstrate the applicability of our pONE vector set.

Indexed as

Genetic VectorsAnimalsAurora Kinase ACloning, MolecularEscherichia coliHEK293 CellsHumansLim KinasesPichiaRecombinant Proteinsrho-Associated KinasesSf9 CellsSpodopteraTransfectionTumor Suppressor ProteinsAURKA protein, humanAurora Kinase ALIMK1 protein, humanLim KinasesRASSF1 protein, humanRecombinant Proteinsrho-Associated KinasesROCK2 protein, humanTumor Suppressor Proteins

Identifiers

PMID31887188
PMCPMC6936851
OpenAlexW2997520606

What OpenQuestion holds

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LicenceCC BY
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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.