Evidence map›Paper›PMID 36323753›Full record

ArticleScientific reports2022

Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems.

Hiroyuki Kajiura, Ken-Ichiro Tatematsu, Tsuyoshi Nomura, Mitsuhiro Miyazawa, Akihiro Usami, Toshiki Tamura, Hideki Sezutsu, Kazuhito Fujiyama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Application of Transgenic Silk Fibroin to Biomaterials.Biotechnology and bioengineering · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. 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

8 authors at 6 institutions in 2 countries.

Hiroyuki Kajiura *International Center for Biotechnology, Osaka University, 2-1 Yamada-Oka, Suita-Shi, Osaka, 565-0871, Japan.
Ken-Ichiro Tatematsu *Division of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki, 305-8634, Japan.
Tsuyoshi Nomura *Sysmex Corporation, 1548 Ooaza Shimookudomi, Sayama, Saitama, 350-1332, Japan.
Mitsuhiro MiyazawaDivision of Biomaterial Sciences, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki, 305-8634, Japan.
Akihiro UsamiSysmex Corporation, 1548 Ooaza Shimookudomi, Sayama, Saitama, 350-1332, Japan.
Toshiki TamuraSilk Science and Technology Research Institute, 1053, Iikura, Ami-Machi, Ibaraki, 300-0324, Japan.
Hideki SezutsuDivision of Silk-Producing Insect Biotechnology, Institute of Agrobiological Sciences, National Agriculture and Food Research Organization, 1-2 Owashi, Tsukuba, Ibaraki, 305-8634, Japan.
Kazuhito FujiyamaInternational Center for Biotechnology, Osaka University, 2-1 Yamada-Oka, Suita-Shi, Osaka, 565-0871, Japan. fujiyama@icb.osaka-u.ac.jp.
Institute of Agrobiological Sciences · JPSysmex (Japan) · JPMahidol University · THNational Agriculture and Food Research Organization · JPOsaka University · JPThe Dainippon Silk Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The silkworm, Bombyx mori, is an attractive host for recombinant protein production due to its high expression efficiency, quality, and quantity. Two expression systems have been widely used for recombinant protein production in B. mori: baculovirus/silkworm expression system and transgenic silkworm expression system. Both expression systems enable high protein production, but the qualities of the resulting recombinant proteins have not been well evaluated. In this study, we expressed bovine interferon γ (IFN-γ) using the two systems and examined the quality of the resulting proteins in terms of N-glycosylation and protein cleavage. Both expression systems successfully produced IFN-γ as an N-glycoprotein. Although the production in the baculovirus/silkworm expression system was much more efficient than that in the transgenic silkworm expression system, unexpected variants of IFN-γ were also produced in the former system due to the different N-glycosylation and C-terminal truncations. These results indicate that while high protein production could be achieved in the baculovirus/silkworm expression system, unintentional protein modification might occur, and therefore protein expression in the transgenic silkworm expression system is preferable from the point-of-view of N-glycosylation of the recombinant protein and evasion of unexpected attack by a protease in B. mori.

Indexed as

BombyxAnimalsAnimals, Genetically ModifiedCattleGlycosylationRecombinant ProteinsRecombinant Proteins

Identifiers

PMID36323753
PMCPMC9628610
OpenAlexW4307921935

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.