ArticleMolecules (Basel, Switzerland)2017
Bacterial Expression of Human Butyrylcholinesterase as a Tool for Nerve Agent Bioscavengers Development.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 36 citations in OpenAlex.
- Dual targeting of iNOS and Src tyrosine kinase as a superior therapeutic strategy against soman-induced long-term neurotoxicity: multimodal biomarker, imaging, and neurobehavioral outcome analyses.Acta neuropathologica communications · 2026Article
- Computational design and experimental characterisation of a stable human heparanase variant.RSC chemical biology · 2022Article
- The structure of natively iodinated bovine thyroglobulin.Acta crystallographica. Section D, Structural biology · 2021Article
- A Thermophilic Bacterial Esterase for Scavenging Nerve Agents: A Kinetic, Biophysical and Structural Study.Molecules (Basel, Switzerland) · 2021Article
- Counteracting poisoning with chemical warfare nerve agents.Arhiv za higijenu rada i toksikologiju · 2020Review
- Practically useful protein-design methods combining phylogenetic and atomistic calculations.Current opinion in structural biology · 2020Review
- Enhancing the Butyrylcholinesterase Activity in HEK-293 Cell Line by Dual-Promoter Vector Decorated on Lipofectamine.Drug design, development and therapy · 2020Article
- Dimerization of human butyrylcholinesterase expressed in bacterium for development of a thermally stable bioscavenger of organophosphorus compounds.Chemico-biological interactions · 2019Article
- Purification of recombinant human butyrylcholinesterase on Hupresin®.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018Article
- Characterization of butyrylcholinesterase from porcine milk.Archives of biochemistry and biophysics · 2018Article
- Optimization of Cholinesterase-Based Catalytic Bioscavengers Against Organophosphorus Agents.Frontiers in pharmacology · 2018Article
- Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.Molecules (Basel, Switzerland) · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human butyrylcholinesterase is a performant stoichiometric bioscavenger of organophosphorous nerve agents. It is either isolated from outdated plasma or functionally expressed in eukaryotic systems. Here, we report the production of active human butyrylcholinesterase in a prokaryotic system after optimization of the primary sequence through the Protein Repair One Stop Shop process, a structure- and sequence-based algorithm for soluble bacterial expression of difficult eukaryotic proteins. The mutant enzyme was purified to homogeneity. Its kinetic parameters with substrate are similar to the endogenous human butyrylcholinesterase or recombinants produced in eukaryotic systems. The isolated protein was prone to crystallize and its 2.5-Å X-ray structure revealed an active site gorge region identical to that of previously solved structures. The advantages of this alternate expression system, particularly for the generation of butyrylcholinesterase variants with nerve agent hydrolysis activity, are discussed.
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