Evidence map›Paper›PMID 24130173›Full record

ArticleBiotechnology journal2014

Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue.

Jeannine D Schneider, Alexandra Castilho, Laura Neumann, Friedrich Altmann, Andreas Loos, Latha Kannan, Tsafrir S Mor, Herta Steinkellner

Abstract read
In one paragraph

Article in Biotechnology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

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  12. Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies.International journal of molecular sciences · 2018
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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 2 institutions in 2 countries.

Jeannine D SchneiderDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Alexandra Castilho
Laura Neumann
Friedrich Altmann
Andreas Loos
Latha Kannan
Tsafrir S Mor
Herta Steinkellner
BOKU University · ATArizona State University · US

Funding

Training and Education CoreU54NS058183 · NINDS · U.S. ARMY MEDICAL RESEARCH INST CHEM DEF · PI CERASOLI, DOUGLAS MARK · 2006 to 2013
$20.6M
Cocaine hydrolase gene therapy for cocaine abuse (DPI)DP1DA031340 · NIDA · MAYO CLINIC ROCHESTER · PI BRIMIJOIN, WILLIAM STEPHEN · 2010 to 2014
$3.9M
Austrian Science Fund FWF L 575Austrian Science Fund FWF W 1224NIDA NIH HHS 1P1DA031340-01NIDA NIH HHS DP1 DA031340NINDS NIH HHS U54 NS058183PHS HHS U-54-NSO58183-01
6 · The paper itself

Abstract

Human butyrylcholinesterase (BChE) is considered a candidate bioscavenger of nerve agents for use in pre- and post-exposure treatment. However, the presence and functional necessity of complex N-glycans (i.e. sialylated structures) is a challenging issue in respect to its recombinant expression. Here we transiently co-expressed BChE cDNA in the model plant Nicotiana benthamiana with vectors carrying the genes necessary for in planta protein sialylation. Site-specific sugar profiling of secreted recombinant BChE (rBChE) collected from the intercellular fluid revealed the presence of mono- and di-sialylated N-glycans, which largely resembles to the plasma-derived orthologue. Attempts to increase that sialylation content of rBChE by the over-expression of an additional glycosylation enzyme that generates branched N-glycans (i.e. β1,4-N-acetylglucosaminyl-transferase IV), allowed the production of rBChE decorated with tri-sialylated structures (up to 70%). Sialylated and non-sialylated plant-derived rBChE exhibited functional in vitro activity comparable to that of its commercially available equine-derived counterpart. These results demonstrate the ability of plants to generate valuable proteins with designed sialylated glycosylation profiles optimized for therapeutic efficacy. Moreover, the efficient synthesis of carbohydrates present only in minute amounts on the native protein (tri-sialylated N-glycans) facilitates the generation of a product with superior efficacies and/or new therapeutic functions.

Indexed as

ButyrylcholinesteraseButyrylthiocholineGlycosylationHumansN-Acetylneuraminic AcidNicotianaPlants, Genetically ModifiedProtein EngineeringRecombinant ProteinsButyrylcholinesteraseButyrylthiocholineN-Acetylneuraminic AcidRecombinant ProteinsButyrylcholinesteraseGlycoengineeringPlantsRecombinant biopharmaceuticalsSialic acid

Identifiers

PMID24130173
PMCPMC3975692
OpenAlexW2117384808

What OpenQuestion holds

Textmetadata
LicenceTDM
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.