2020
DOI: 10.1007/s00449-020-02457-8
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Expression of porcine interferon-α and its bioactivity analysis in vitro and in vivo

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Cited by 3 publications
(5 citation statements)
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“…In previous reports, poIFN-α was expressed in the Pichia pastoris system, the baculovirus system and the E. coli expression system (Mallick et al 2011 ; Huang et al 2012 ; Wang et al 2021 ). For mammalian cell expression systems and Pichia pastoris systems, culture is very time-consuming and expensive, the yield of recombinant proteins is very low, and the purification process is relatively complicated.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…In previous reports, poIFN-α was expressed in the Pichia pastoris system, the baculovirus system and the E. coli expression system (Mallick et al 2011 ; Huang et al 2012 ; Wang et al 2021 ). For mammalian cell expression systems and Pichia pastoris systems, culture is very time-consuming and expensive, the yield of recombinant proteins is very low, and the purification process is relatively complicated.…”
Section: Discussionmentioning
confidence: 99%
“…Compared with other expression systems, the E. coli expression systems offer several advantages for protein production, such as high yields, low costs, and rapid expression. Wang et al successfully expressed recombinant poIFN-α with high bioactivity in E. coli (Wang et al 2021 ). PoIFN-α that was cloned and expressed in E. coli.…”
Section: Discussionmentioning
confidence: 99%
“…On the contrary, little if any activity was shown by IFN-a3, -a7, -a13, -a4 and -a15 [4]. Accordingly, minor differences of the aminoacid sequence can account for dramatic increases in antiviral activity: the mutant PoIFN-α-156s inhibits much more PRV replication in a dose-dependent manner in vitro, compared with the original PoIFN-α [218]. Among IFN-stimulated genes, ISG15 [219] and ISG20 [220] probably play a major role in regulating the antiviral control activities.…”
Section: Ifn Sensitivity Of Prvmentioning
confidence: 99%
“…al. 2011;Huang et al 2012;Wang et al 2021). For mammalian cell expression systems and Pichia pastoris systems, culture is very time-consuming and expensive, the yield of recombinant proteins is very low, and the puri cation process is relatively complicated.…”
mentioning
confidence: 99%
“…Compared with other expression systems, E. coli expression systems offer several advantages for protein production, such as high yields, low costs, and rapid expression. Wang et al successfully expressed recombinant porcine IFN-α with high bioactivity in E. coli(Wang et al 2021). Porcine IFN-α was also cloned and expressed in E. coli.…”
mentioning
confidence: 99%