Evidence map›Paper›PMID 27029048›Full record

ArticlePloS one2016

Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems.

Raphael Reuten, Denise Nikodemus, Maria B Oliveira, Trushar R Patel, Bent Brachvogel, Isabelle Breloy, Jörg Stetefeld, Manuel Koch

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  13. Acentrosomal spindle assembly and maintenance inMolecular biology of the cell · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Mammalian Expression andACS omega · 2020
    Article
  19. Article
  20. Alkyltransferase-like protein clusters scan DNA rapidly over long distances and recruit NER to alkyl-DNA lesions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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 4 institutions in 4 countries.

Raphael ReutenInstitute for Dental Research and Oral Musculoskeletal Biology, Medical Faculty, University of Cologne, Cologne, Germany.
Denise NikodemusInstitute for Dental Research and Oral Musculoskeletal Biology, Medical Faculty, University of Cologne, Cologne, Germany.
Maria B OliveiraCenter for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Trushar R PatelDepartment of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada.
Bent BrachvogelCenter for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Isabelle BreloyCenter for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Jörg StetefeldDepartment of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba RT3 2N2, Canada.
Manuel KochInstitute for Dental Research and Oral Musculoskeletal Biology, Medical Faculty, University of Cologne, Cologne, Germany.
University of Cologne · DEUniversity of Birmingham · GBUniversity of Lisbon · PTUniversity of Manitoba · CA

Funding

Canadian Institutes of Health Research RPA-109759
6 · The paper itself

Abstract

Recombinant proteins are commonly expressed in eukaryotic expression systems to ensure the formation of disulfide bridges and proper glycosylation. Although many proteins can be expressed easily, some proteins, sub-domains, and mutant protein versions can cause problems. Here, we investigated expression levels of recombinant extracellular, intracellular as well as transmembrane proteins tethered to different polypeptides in mammalian cell lines. Strikingly, fusion of proteins to the prokaryotic maltose-binding protein (MBP) generally enhanced protein production. MBP fusion proteins consistently exhibited the most robust increase in protein production in comparison to commonly used tags, e.g., the Fc, Glutathione S-transferase (GST), SlyD, and serum albumin (ser alb) tag. Moreover, proteins tethered to MBP revealed reduced numbers of dying cells upon transient transfection. In contrast to the Fc tag, MBP is a stable monomer and does not promote protein aggregation. Therefore, the MBP tag does not induce artificial dimerization of tethered proteins and provides a beneficial fusion tag for binding as well as cell adhesion studies. Using MBP we were able to secret a disease causing laminin β2 mutant protein (congenital nephrotic syndrome), which is normally retained in the endoplasmic reticulum. In summary, this study establishes MBP as a versatile expression tag for protein production in eukaryotic expression systems.

Indexed as

AnimalsCell AdhesionCell Line, TumorGene ExpressionGreen Fluorescent ProteinsHEK293 CellsHumansMaltose-Binding ProteinsMiceRecombinant Fusion Proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsMaltose-Binding ProteinsRecombinant Fusion Proteins

Identifiers

PMID27029048
PMCPMC4814134
OpenAlexW2328165382

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.