About: Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease

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About: Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease 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	Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease
Creator	Domínguez, Elvira Xie, Qi Zhang, Zhonghui Zheng, Nuoyan De Jesú S Pérez, José Garcia, Juan
Source	Elsevier; Medline; PMC
abstract	Abstract Site-specific proteases are the most popular kind of enzymes for removing the fusion tags from fused target proteins. Nuclear inclusion protein a (NIa) proteases obtained from the family Potyviridae have become promising due to their high activities and stringencies of sequences recognition. NIa proteases from tobacco etch virus (TEV) and tomato vein mottling virus (TVMV) have been shown to process recombinant proteins successfully in vitro. In this report, recombinant PPV (plum pox virus) NIa protease was employed to process fusion proteins with artificial cleavage site in vitro. Characteristics such as catalytic ability and affecting factors (salt, temperature, protease inhibitors, detergents, and denaturing reagents) were investigated. Recombinant PPV NIa protease expressed and purified from Escherichia coli demonstrated efficient and specific processing of recombinant GFP and SARS-CoV nucleocapsid protein, with site F (N V V V H Q▾A) for PPV NIa protease artificially inserted between the fusion tags and the target proteins. Its catalytic capability is similar to those of TVMV and TEV NIa protease. Recombinant PPV NIa protease reached its maximal proteolytic activity at approximately 30°C. Salt concentration and only one of the tested protease inhibitors had minor influences on the proteolytic activity of PPV NIa protease. Recombinant PPV NIa protease was resistant to self-lysis for at least five days.
has issue date	2008-02-29(xsd:dateTime)
bibo:doi	10.1016/j.pep.2007.10.008
bibo:pmid	18024078
has license	els-covid
sha1sum (hex)	9d4858b586fae5f028cbdc63f3989a9095d7b1d8
schema:url	https://doi.org/10.1016/j.pep.2007.10.008
resource representing a document's title	Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease
has PubMed Central identifier	PMC7130002
has PubMed identifier	18024078
schema:publication	Protein Expression and Purification
resource representing a document's body	covid:9d4858b586fae5f028cbdc63f3989a9095d7b1d8#body_text
is schema:about of	named entity 'NIA' named entity 'expressed' named entity 'activity' named entity 'Characteristics' named entity 'proteolytic' named entity 'protease' named entity 'maximal' named entity 'GFP' named entity 'promising' named entity 'fusion proteins' named entity 'PLUM POX VIRUS' named entity 'FUSION' named entity 'CAPABILITY' named entity 'INVESTIGATED' named entity 'DEMONSTRATED' named entity 'FUSION' named entity 'REPORT' named entity 'CONCENTRATION' named entity 'NUCLEAR INCLUSION' named entity 'DAYS' named entity 'RECOGNITION' named entity 'POX VIRUS' named entity 'GFP' named entity 'PROTEASE INHIBITORS' named entity 'PROTEIN A' named entity 'ONE OF' covid:arg/9d4858b586fae5f028cbdc63f3989a9095d7b1d8 named entity 'CATALYTIC' named entity 'FAMILY' named entity 'TOBACCO ETCH VIRUS' named entity 'VEIN' named entity 'PURIFIED' named entity 'SELF' named entity 'MOTTLING' named entity 'RESISTANT TO' named entity 'IN VITRO' named entity 'KIND' named entity 'REAGENTS' named entity 'TARGET' named entity 'RECOMBINANT PROTEINS' named entity 'TOMATO' named entity 'SPECIFIC' named entity 'HAVE' named entity 'EMPLOYED' named entity 'ESCHERICHIA COLI' named entity 'PROTEASE' named entity 'EFFICIENT' named entity 'SITE' named entity 'TAGS' named entity 'AFFECTING' named entity '30%' named entity 'RECOMBINANT' named entity 'PROTEINS' named entity 'SPECIFIC' named entity 'PROTEASE' named entity 'HIGH' named entity 'PPV' named entity 'FUSED' named entity 'OBTAINED' named entity 'DETERGENTS' named entity 'VIRUS' named entity 'CLEAVAGE' named entity 'NIA' named entity 'REMOVING' named entity 'PROTEOLYTIC ACTIVITY' named entity 'LYSIS' named entity 'APPROXIMATELY' named entity 'PROTEASES' named entity 'EFFICIENT' named entity 'DUE TO' named entity 'PROCESSING' named entity 'ACTIVITIES' named entity 'ITS' named entity 'PROCESS' named entity 'DENATURING' named entity 'SALT'

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