About: Recombinant Scorpine Produced Using SUMO Fusion Partner in Escherichia coli Has the Activities against Clinically Isolated Bacteria and Inhibits the Plasmodium falciparum Parasitemia In Vitro

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About: Recombinant Scorpine Produced Using SUMO Fusion Partner in Escherichia coli Has the Activities against Clinically Isolated Bacteria and Inhibits the Plasmodium falciparum Parasitemia In Vitro Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Recombinant Scorpine Produced Using SUMO Fusion Partner in Escherichia coli Has the Activities against Clinically Isolated Bacteria and Inhibits the Plasmodium falciparum Parasitemia In Vitro
Creator	Zhang, Chao Cao, Jun Gao, Qi Zhou, Huayun Gu, Yaping He, Xinlong
topic	covid:7db22f7f81977109d493a0edf8ed75562648e839#this
Source	PMC
abstract	Scorpine, a small cationic peptide from the venom of Pandinus imperator, which has been shown to have anti-bacterial and anti-plasmodial activities, has potential important applications in the pharmaceutical industries. However, the isolation of scorpine from natural sources is inefficient and time-consuming. Here, we first report the expression and purification of recombinant scorpine in Escherichia coli, using small ubiquitin-related modifier (SUMO) fusion partner. The fusion protein was expressed in soluble form in E. coli, and expression was verified by SDS-PAGE and western blotting analysis. The fusion protein was purified to 90% purity by nickel–nitrilotriacetic acid (Ni(2+)–NTA) resin chromatography. After the SUMO-scorpine fusion protein was cleaved by the SUMO protease, the cleaved sample was reapplied to a Ni(2+)–NTA column. Tricine/SDS-PAGE gel results indicated that Scorpine had been purified successfully to more than 95% purity. The recombinantly expressed Scorpine showed anti-bacterial activity against two standard bacteria including Staphylococcus aureus ATCC 29213 and Acinetobacter baumannii ATCC 19606, and clinically isolated bacteria including S. aureus S, S. aureus R, A. baumannii S, and A. baumannii R. It also produced 100% reduction in Plasmodium falciparum parasitemia in vitro. Thus, the expression strategy presented in this study allowed convenient high yield and easy purification of recombinant Scorpine for pharmaceutical applications in the future.
has issue date	2014-07-28(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0103456
bibo:pmid	25068263
has license	cc-by
sha1sum (hex)	7db22f7f81977109d493a0edf8ed75562648e839
schema:url	https://doi.org/10.1371/journal.pone.0103456
resource representing a document's title	Recombinant Scorpine Produced Using SUMO Fusion Partner in Escherichia coli Has the Activities against Clinically Isolated Bacteria and Inhibits the Plasmodium falciparum Parasitemia In Vitro
has PubMed Central identifier	PMC4113386
has PubMed identifier	25068263
schema:publication	PLoS One
resource representing a document's body	covid:7db22f7f81977109d493a0edf8ed75562648e839#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/7db22f7f81977109d493a0edf8ed75562648e839
is schema:about of	named entity 'IN VITRO' named entity 'presented' named entity 'recombinant' named entity '2014' named entity 'Parasitemia' named entity 'falciparum' named entity 'Vitro' named entity 'NTA' named entity 'ACINETOBACTER BAUMANNII' named entity 'RECOMBINANT' named entity 'FUSION' named entity 'WESTERN BLOTTING' named entity 'SDS-PAGE' named entity 'ACTIVITIES' named entity 'S. AUREUS' named entity 'VERIFIED' named entity 'FUSION PROTEIN' named entity 'CHROMATOGRAPHY' named entity 'FUTURE' named entity 'PROTEIN ' named entity 'CLEAVED' named entity 'ZHOU' named entity 'STRATEGY' named entity 'REDUCTION' named entity 'TRICINE' named entity 'PAGE' named entity 'SCORPINE' named entity 'PARTNER' named entity 'NATURAL' named entity '100%' named entity 'EXPRESSION' named entity 'EASY' named entity 'CONVENIENT' named entity 'PHARMACEUTICAL INDUSTRIES' named entity 'PHARMACEUTICAL' named entity 'SUMO' named entity 'ISOLATED' named entity 'USING' named entity 'ESCHERICHIA COLI' named entity 'SCORPINE' named entity 'PURIFICATION' named entity 'ANALYSIS' named entity '90%' named entity 'HERE' named entity 'INCLUDING' named entity 'SOLUBLE FORM' named entity 'MORE THAN' named entity 'BACTERIA ' named entity 'PARTNER' named entity 'PLASMODIUM FALCIPARUM PARASITEMIA' named entity 'SAMPLE' named entity 'USING' named entity 'TIME-CONSUMING' named entity 'STAPHYLOCOCCUS AUREUS' named entity 'INDICATED' named entity 'RESULTS' named entity 'ISOLATION' named entity 'ACTIVITIES' named entity 'VENOM' named entity 'PURIFIED' named entity 'MODIFIER' named entity 'HIGH YIELD' named entity 'CITATION' named entity 'STANDARD' named entity 'UBIQUITIN-RELATED' named entity 'BACTERIAL ACTIVITY' named entity 'STUDY' named entity 'REPORT' named entity '287' named entity '19606' named entity 'ALLOWED' named entity 'SOURCES' named entity 'PEPTIDE' named entity 'RECOMBINANT'

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