Evidence map›Paper›PMID 32766842›Full record

ArticleJournal of biochemistry2021

Structural insight and stability of TNFR-Fc fusion protein (Etanercept) produced by using transgenic silkworms.

Masato Kiyoshi, Ken-Ichiro Tatematsu, Minoru Tada, Hideki Sezutsu, Hiroko Shibata, Akiko Ishii-Watabe

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

6 authors at 2 institutions in 1 country.

Masato KiyoshiDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa 210-9501, Japan.
Ken-Ichiro TatematsuTransgenic Silkworm Research Unit, National Institute of Agrobiological Sciences National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan.
Minoru TadaDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa 210-9501, Japan.
Hideki SezutsuTransgenic Silkworm Research Unit, National Institute of Agrobiological Sciences National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki 305-8634, Japan.
Hiroko ShibataDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa 210-9501, Japan.
Akiko Ishii-WatabeDivision of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa 210-9501, Japan.
National Institute of Health Sciences · JPNational Agriculture and Food Research Organization · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Therapeutic proteins expressed using transgenic animals have been of great interest for several years. Especially, transgenic silkworm has been studied intensively because of its ease in handling, low-cost, high-yield and unique glycosylation patterns. However, the physicochemical property of the therapeutic protein expressed in transgenic silkworm remains elusive. Here, we constructed an expression system for the TNFR-Fc fusion protein (Etanercept) using transgenic silkworm. The TNFR-Fc fusion protein was employed to N-glycan analysis, which revealed an increased amount of afucosylated protein. Evidence from surface plasmon resonance analysis showed that the TNFR-Fc fusion protein exhibit increased binding affinity for Fcγ receptor IIIa and FcRn compared to the commercial Etanercept, emphasizing the profit of expression system using transgenic silkworm. We have further discussed the comparison of higher order structure, thermal stability and aggregation of the TNFR-Fc fusion protein.

Indexed as

AnimalsAnimals, Genetically ModifiedBombyxCHO CellsCricetulusEtanerceptGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GProtein StabilityRecombinant Fusion ProteinsTumor Necrosis Factor-alphaEtanerceptImmunoglobulin Fc FragmentsImmunoglobulin GRecombinant Fusion ProteinsTumor Necrosis Factor-alphaFc fusion proteinglycosylationphysicochemical propertysilkwormtherapeutic protein

Identifiers

PMID32766842
PMCPMC7868081
OpenAlexW3047916695

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.