About: Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli

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About: Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli
Creator	Cho, Chong-Su Choi, Yun-Jaie Bok, Jin-Duck Hong, Zhong-Shan Kang, Sang-Kee Kim, In-Seon Lee, Yoon-Seok Li, Hui-Shan Oh, Seo-Ho Piao, Da-Chuan Shin, Do-Woon Singh, Bijay Maharjan, S
source	Medline; PMC
abstract	BACKGROUND: Porcine epidemic diarrhea virus (PEDV) is a highly contagious enteric pathogen of swine. The spike glycoprotein (S) of PEDV is the major immunogenic determinant that plays a pivotal role in the induction of neutralizing antibodies against PEDV, which therefore is an ideal target for the development of subunit vaccine. In an attempt to develop a subunit vaccine for PEDV, we cloned two different fragments of S protein and expressed as glutathione S-transferase (GST)-tagged fusion proteins, namely rGST-COE and rGST-S1D, in E.coli. However, the expression of these recombinant protein antigens using a variety of expression vectors, strains, and induction conditions invariably resulted in inclusion bodies. To achieve the soluble expression of recombinant proteins, several chaperone co-expression systems were tested in this study. RESULTS: We firstly tested various chaperone co-expression systems and found that co-expression of trigger factor (TF) with recombinant proteins at 15 °C was most useful in soluble production of rGST-COE and rGST-S1D compared to GroEL-ES and DnaK-DnaJ-GrpE/GroEL-ES systems. The soluble rGST-COE and rGST-S1D were purified using glutathione Sepharose 4B with a yield of 7.5 mg/l and 5 mg/l, respectively. Purified proteins were detected by western blot using mouse anti-GST mAb and pig anti-PEDV immune sera. In an indirect ELISA, purified proteins showed immune reactivity with pig anti-PEDV immune sera. Finally, immunization of mice with 10 μg of purified proteins elicited highly potent serum IgG and serum neutralizing antibody titers. CONCLUSIONS: In this study, soluble production of recombinant spike protein of PEDV, rGST-COE and rGST-S1D, were achieved by using TF chaperone co-expression system. Our results suggest that soluble rGST-COE and rGST-S1D produced by co-expressing chaperones may have the potential to be used as subunit vaccine antigens. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12896-016-0268-7) contains supplementary material, which is available to authorized users.
has issue date	2016-05-04(xsd:dateTime)
bibo:doi	10.1186/s12896-016-0268-7
bibo:pmid	27142206
has license	cc-by
sha1sum (hex)	1e2493a8e26be4ff934b96dedc32dc7cf5728370
schema:url	https://doi.org/10.1186/s12896-016-0268-7
resource representing a document's title	Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli
has PubMed Central identifier	PMC4855837
has PubMed identifier	27142206
schema:publication	BMC Biotechnol
resource representing a document's body	covid:1e2493a8e26be4ff934b96dedc32dc7cf5728370#body_text
is schema:about of	named entity 'USEFUL' named entity 'IMMUNE' named entity 'SOLUBLE' named entity 'GST' named entity 'CHAPERONE' named entity 'PATHOGEN' named entity 'MAJOR' named entity 'ANTIBODY TITERS' named entity 'DETERMINANT' named entity 'IDEAL' named entity 'MAB' named entity 'INDIRECT' named entity 'SERUM' named entity 'GLUTATHIONE' named entity 'EXPRESSED' named entity 'CO-EXPRESSION' named entity 'INCLUSION BODIES' named entity 'RECOMBINANT PROTEIN' named entity 'MG%' named entity 'NEUTRALIZING ANTIBODIES' named entity 'yield' named entity 'highly' named entity 'co-expression' named entity 'plays' named entity 'immune sera' named entity 'neutralizing antibody' named entity 'Trigger' named entity 'PROTEIN ' named entity 'ANTIGENS' named entity 'STRAINS' named entity 'YIELD' named entity 'INDUCTION' named entity 'DEVELOPMENT' named entity 'IMMUNE SERA' named entity 'PURIFIED' named entity 'IMMUNIZATION' named entity 'CONDITIONS' named entity 'GRPE' named entity 'PIG' named entity 'STUDY' named entity 'ENTERIC' named entity 'PLAYS' named entity 'VARIOUS' named entity 'MICE' named entity 'PRODUCTION' named entity 'DNAK' named entity 'TAGGED' named entity 'ROLE' named entity 'RECOMBINANT PROTEINS' named entity 'HIGHLY' named entity 'THESE' named entity 'IS A' named entity 'GROEL' named entity 'GLUTATHIONE S-TRANSFERASE' named entity 'SPIKE PROTEIN' named entity 'RECOMBINANT' named entity 'PROTEIN ' named entity 'PORCINE EPIDEMIC DIARRHEA VIRUS' named entity 'EXPRESSION' named entity 'DETECTED' named entity 'DIFFERENT' named entity 'TRIGGER FACTOR' named entity 'BACKGROUND' named entity 'PORCINE EPIDEMIC DIARRHEA VIRUS' named entity 'E.COLI' named entity 'FOUND' named entity 'COMPARED' named entity '28S' named entity 'S PROTEIN'

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