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Expression of SARS-CoV-2 Nucleocapsid (N) Recombinant Protein Using Escherichia coli System

HAYATI Journal of Biosciences · Vol. 30 No. 3 (2023) · hlm. 445–450

DOI
10.4308/hjb.30.3.445-450
ISSN
2086-4094, 1978-3019
Terbit
2023-01-19
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng

Abstrak

One of the main antigen that can be used for serological testing is the nucleocapsid (N) which is the most abundant viral-derived protein in SARS-CoV-2 where this virus can cause COVID19 disease. The aim of this study was to develop the SARS-CoV-2 N recombinant protein using Escherichia coli expression system. A total of 1,089 nucleotides encoding 362 amino acids of SARS-CoV-2 N was cloned to pET-14b vector. The plasmid then expressed in E. coli BL21 (DE3) and induced with 1.0 mM IPTG (Isopropyl-β-d-1-thiogalactopyranoside). The cell was harvested using denaturation lysis buffer due to inclusion body formation of SARS-CoV-2 N protein. Dialysis processed and concentrated using PEG-6000 resulted 0.992 mg/ml protein yield. Analysis of SARS-CoV-2 N recombinant protein using SDS-PAGE technique showed approximately 37.0 kDa specific band target protein. Application of this SARS-CoV-2 N recombinant protein to vaccinated and non-vaccinated antibody serum samples using ELISA technique indicated the significant result of optical density mean at 0.603 and 0.135, respectively. This study revealed that the production of SARS-COV-2 N recombinant protein could be carried out in E. coli expression system under denatured conditions, therefore the methods are more effective in producing the protein as a basic material in immuno-diagnostic assay.

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Sumber metadata: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/hayati/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en">Expression of SARS-CoV-2 Nucleocapsid (N) Recombinant Protein Using Escherichia coli System</dc:title>
	<dc:creator xml:lang="en">Ansari, Rizki Aulia</dc:creator>
	<dc:creator xml:lang="en">Saepuloh, Uus</dc:creator>
	<dc:creator xml:lang="en">Mariya, Silmi</dc:creator>
	<dc:creator xml:lang="en">Yuliana</dc:creator>
	<dc:creator xml:lang="en">Noviana, Rachmitasari</dc:creator>
	<dc:creator xml:lang="en">Suparto, Irma Herawati</dc:creator>
	<dc:creator xml:lang="en">Darusman, Huda Shalahudin</dc:creator>
	<dc:description xml:lang="en">One of the main antigen that can be used for serological testing is the nucleocapsid (N) which is the most abundant viral-derived protein in SARS-CoV-2 where this virus can cause COVID19 disease. The aim of this study was to develop the SARS-CoV-2 N recombinant protein using Escherichia coli expression system. A total of 1,089 nucleotides encoding 362 amino acids of SARS-CoV-2 N was cloned to pET-14b vector. The plasmid then expressed in E. coli BL21 (DE3) and induced with 1.0 mM IPTG (Isopropyl-β-d-1-thiogalactopyranoside). The cell was harvested using denaturation lysis buffer due to inclusion body formation of SARS-CoV-2 N protein. Dialysis processed and concentrated using PEG-6000 resulted 0.992 mg/ml protein yield. Analysis of SARS-CoV-2 N recombinant protein using SDS-PAGE technique showed approximately 37.0 kDa specific band target protein. Application of this SARS-CoV-2 N recombinant protein to vaccinated and non-vaccinated antibody serum samples using ELISA technique indicated the significant result of optical density mean at 0.603 and 0.135, respectively. This study revealed that the production of SARS-COV-2 N recombinant protein could be carried out in E. coli expression system under denatured conditions, therefore the methods are more effective in producing the protein as a basic material in immuno-diagnostic assay.</dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2023-01-19</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en">Peer-reviewed Article</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>http://journal.ipb.ac.id/hayati/article/view/40476</dc:identifier>
	<dc:identifier>10.4308/hjb.30.3.445-450</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 30 No. 3 (2023): May 2023; 445-450</dc:source>
	<dc:source>2086-4094</dc:source>
	<dc:source>1978-3019</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>http://journal.ipb.ac.id/hayati/article/view/40476/24833</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2023 Rizki Aulia Ansari, Uus Saepuloh, Silmi Mariya, Yuliana, Rachmitasari Noviana, Irma Herawati Suparto, Huda Shalahudin Darusman</dc:rights>
</oai_dc:dc>