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. 2020 Apr 19;8(2):190. doi: 10.3390/vaccines8020190

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Generation, purification, and MAb recognition of nucleocapsid-like particles (NLP)-recombinant proteins. (a) Schematic representation of P. vivax circumsporozoite (PvCSP) proteins fused with mumps virus nucleocapsid expressed from P. pastoris. (b) NLP-CSP_CT and NLP-CSP_R are represented as lines 1 and 2, respectively. SDS-PAGE analysis under reducing conditions of purified recombinant proteins gel-stained with Coomassie blue (1 µg of protein per lane) and protein recognition by mAbs anti-VK210, anti-VK247, and anti-NP, and by polyclonal anti-P. vivax-like antibody. (c) The purity of the proteins after chromatography was analyzed by RP-HPLC, in which the gradient elution was developed by combining 0.1% trifluoroacetic acid (TFA) in water and 0.1% TFA in 90% acetonitrile at 24 °C, 1 mL/min for 40 min in a C18 column.

Generation, purification, and MAb recognition of nucleocapsid-like particles (NLP)-recombinant proteins. (a) Schematic representation of P. vivax circumsporozoite (PvCSP) proteins fused with mumps virus nucleocapsid expressed from P. pastoris. (b) NLP-CSP_CT and NLP-CSP_R are represented as lines 1 and 2, respectively. SDS-PAGE analysis under reducing conditions of purified recombinant proteins gel-stained with Coomassie blue (1 µg of protein per lane) and protein recognition by mAbs anti-VK210, anti-VK247, and anti-NP, and by polyclonal anti-P. vivax-like antibody. (c) The purity of the proteins after chromatography was analyzed by RP-HPLC, in which the gradient elution was developed by combining 0.1% trifluoroacetic acid (TFA) in water and 0.1% TFA in 90% acetonitrile at 24 °C, 1 mL/min for 40 min in a C18 column.