2014
DOI: 10.1016/j.ijbiomac.2014.03.043
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Expression, purification and antibody preparation using different constructs of PCV2 capsid protein

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Cited by 16 publications
(11 citation statements)
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“…Epitope prediction strongly indicated presence of a potential linear epitope in the NLS of PCV3 Cap (Additional file 1: Table S1 and Figure S1). In contrast, the NLS of PCV2 Cap contains an important epitope, whereas removal of the NLS from the Cap dramatically increased expression level of this protein in bacteria [28, 29]. We also tried to express full-length PCV3 Cap in bacteria using codon-optimized cap genes, but no protein of interest was detected in cell lysates (data not shown).…”
Section: Discussionmentioning
confidence: 99%
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“…Epitope prediction strongly indicated presence of a potential linear epitope in the NLS of PCV3 Cap (Additional file 1: Table S1 and Figure S1). In contrast, the NLS of PCV2 Cap contains an important epitope, whereas removal of the NLS from the Cap dramatically increased expression level of this protein in bacteria [28, 29]. We also tried to express full-length PCV3 Cap in bacteria using codon-optimized cap genes, but no protein of interest was detected in cell lysates (data not shown).…”
Section: Discussionmentioning
confidence: 99%
“…Therefore, both the NLS-truncated and the full-length Caps may have different reactions with PCV3 antibody in pig serum. Interestingly, a peptide (aa 17–50) located within the NLS of PCV2 Cap was speculated to be an important epitope in a previous report [28]. Later, a core epitope ( 26 RPWLVHPRHRY 36 ) located in the NLS region of PCV2 Cap was also identified by monoclonal antibodies [29].…”
Section: Introductionmentioning
confidence: 99%
“…PCV2 Cap, Rep and ORF3 proteins were prepared and purified according to the protocols described previously [ 6 , 7 ]. Briefly, the ΔCap17–233 with truncated version of the Cap gene lacking the 5′-end 48 nt encoding the N-terminal 16 amino acid residues was amplified and subcloned into the expression vector pET28b (+) (Novagene, Germany) to generate recombinant expression plasmids pET28b-ΔCap17–233.…”
Section: Methodsmentioning
confidence: 99%
“…Based on current knowledge, many documents were reported either based on inactivated PCV2 or PCV2 subunit proteins [ 6 9 ]. However, few studies were reported to compare the efficiency of inactivated PCV2 and PCV2 subunit proteins.…”
Section: Introductionmentioning
confidence: 99%
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