Evidence map›Paper›PMID 30468023›Full record

ArticlePlant biotechnology journal2019

Cost-effective production of tag-less recombinant protein in Nicotiana benthamiana.

Md Reyazul Islam, Ju-Won Kwak, Jeon-Soo Lee, Sung-Wook Hong, Md Rezaul Islam Khan, Yongjik Lee, Yoontae Lee, Seung-Woo Lee, Inhwan Hwang

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Transient expression of human interleukin-15 inPlant biotechnology (Tokyo, Japan) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Expression of kiwifruit-derived actinidin inFrontiers in plant science · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Rewiring cell-free metabolic flux inSynthetic biology (Oxford, England) · 2023
    Article
  18. Review
  19. Article
  20. Review
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 at 1 institution in 1 country.

Md Reyazul IslamDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Korea.ORCID 0000-0001-9494-3197
Ju-Won KwakDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Korea.
Jeon-Soo LeeDepartment of Life Science, Pohang University of Science and Technology, Pohang, Korea.
Sung-Wook HongDepartment of Life Science, Pohang University of Science and Technology, Pohang, Korea.
Md Rezaul Islam KhanDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Korea.
Yongjik LeeDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Korea.
Yoontae LeeDepartment of Life Science, Pohang University of Science and Technology, Pohang, Korea.
Seung-Woo LeeDepartment of Life Science, Pohang University of Science and Technology, Pohang, Korea.
Inhwan HwangDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Korea.ORCID 0000-0002-1388-1367
Pohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants have recently received a great deal of attention as a means of producing recombinant proteins. Despite this, a limited number of recombinant proteins are currently on the market and, if plants are to be more widely used, a cost-effective and efficient purification method is urgently needed. Although affinity tags are convenient tools for protein purification, the presence of a tag on the recombinant protein is undesirable for many applications. A cost-effective method of purification using an affinity tag and the removal of the tag after purification has been developed. The family 3 cellulose-binding domain (CBM3), which binds to microcrystalline cellulose, served as the affinity tag and the small ubiquitin-related modifier (SUMO) and SUMO-specific protease were used to remove it. This method, together with size-exclusion chromatography, enabled purification of human interleukin-6 (hIL6) with a yield of 18.49 mg/kg fresh weight from leaf extracts of Nicotiana benthamiana following Agrobacterium-mediated transient expression. Plant-produced hIL6 (P-hIL6) contained less than 0.2 EU/μg (0.02 ng/mL) endotoxin. P-hIL6 activated the Janus kinase-signal transducer and activator of transcriptional pathways in human LNCaP cells, and induced expression of IL-21 in activated mouse CD4

Indexed as

BiotechnologyInterleukin-6NicotianaRecombinant ProteinsAnimalsCells, CulturedChromatography, AffinityHumansMicePlant LeavesIL6 protein, humanInterleukin-6Recombinant ProteinsbdSENP1bdSUMOcellulose-binding domainhuman interleukin-6Nicotiana benthamianaplant-based expression systemproteolytic tag removal

Identifiers

PMID30468023
PMCPMC6523591
OpenAlexW2901043781

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.