Evidence map›Paper›PMID 23065352›Full record

ArticleGlycobiology2013

Impact of a human CMP-sialic acid transporter on recombinant glycoprotein sialylation in glycoengineered insect cells.

Hideaki Mabashi-Asazuma, Xianzong Shi, Christoph Geisler, Chu-Wei Kuo, Kay-Hooi Khoo, Donald L Jarvis

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Sialylation and sialyltransferase in insects.Glycoconjugate journal · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Humanizing glycosylation pathways in eukaryotic expression systems.World journal of microbiology & biotechnology · 2017
    Review
  10. Review
  11. Article
  12. Using glyco-engineering to produce therapeutic proteins.Expert opinion on biological therapy · 2015
    Review
  13. Article
  14. Article
  15. 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 2 countries.

Hideaki Mabashi-AsazumaDepartment of Molecular Biology, University of Wyoming, Laramie, WY 82071, USA.
Xianzong Shi
Christoph Geisler
Chu-Wei Kuo
Kay-Hooi Khoo
Donald L Jarvis
University of Wyoming · USInstitute of Biological Chemistry, Academia Sinica · TW

Funding

N-GLYCOSYLATION MECHANISM IN INSECT CELLSR01GM049734 · NIGMS · UNIVERSITY OF WYOMING · PI JARVIS, DONALD L. · 1994 to 2010
$2.7M
NIGMS NIH HHS R01 GM049734NIGMS NIH HHS R01GM49734
6 · The paper itself

Abstract

Insect cells are widely used for recombinant glycoprotein production, but they cannot provide the glycosylation patterns required for some biotechnological applications. This problem has been addressed by genetically engineering insect cells to express mammalian genes encoding various glycoprotein glycan processing functions. However, for various reasons, the impact of a mammalian cytosine-5'-monophospho (CMP)-sialic acid transporter has not yet been examined. Thus, we transformed Spodoptera frugiperda (Sf9) cells with six mammalian genes to generate a new cell line, SfSWT-4, that can produce sialylated glycoproteins when cultured with the sialic acid precursor, N-acetylmannosamine. We then super-transformed SfSWT-4 with a human CMP-sialic acid transporter (hCSAT) gene to isolate a daughter cell line, SfSWT-6, which expressed the hCSAT gene in addition to the other mammalian glycogenes. SfSWT-6 cells had higher levels of cell surface sialylation and also supported higher levels of recombinant glycoprotein sialylation, particularly when cultured with low concentrations of N-acetylmannosamine. Thus, hCSAT expression has an impact on glycoprotein sialylation, can reduce the cost of recombinant glycoprotein production and therefore should be included in ongoing efforts to glycoengineer the baculovirus-insect cell system. The results of this study also contributed new insights into the endogenous mechanism and potential mechanisms of CMP-sialic acid accumulation in the Golgi apparatus of lepidopteran insect cells.

Indexed as

GlycoproteinsGlycosylationN-Acetylneuraminic AcidAnimalsCell LineCytidine Monophosphate N-Acetylneuraminic AcidGenetic VectorsHexosaminesHumansInsectaNucleotide Transport ProteinsOrganic Anion TransportersProtein Processing, Post-TranslationalRecombinant ProteinsSpodopteraSymportersCytidine Monophosphate N-Acetylneuraminic AcidGlycoproteinsHexosaminesN-acetylmannosamineN-Acetylneuraminic AcidNucleotide Transport ProteinsOrganic Anion TransportersRecombinant Proteinssialic acid transport proteinsSLC35A1 protein, humanSymporters

Identifiers

PMID23065352
PMCPMC3531296
OpenAlexW2149961418

What OpenQuestion holds

Textmetadata
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.