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Foldon fusion of RBD and S1 fragments of SARS‐CoV‐2 to stabilize the structure of subunit protein as a vaccine candidate

Indonesian Journal of Biotechnology · Vol. 28 No. 3 (2023) · hlm. 173–179

DOI
10.22146/ijbiotech.82159
ISSN
2089-2241, 0853-8654
Terbit
2023-09-30
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

The COVID‐19 pandemic threatened public health around the world at the same time as highlighting the urgency of vaccine development. Subunit vaccines are safe and effective vaccine types that utilize parts of viruses to trigger the body’s immune response. Previous research has shown that fusion of the spike protein with the foldon domain (fd) achieved the trimeric form to increase the protein stability of the recombinant subunit protein spike from SARS‐CoV and MERS‐CoV, thus exceeding the immune response in the body. The study aims to observe the expression of RBD‐fd and S1‐fd recombinant proteins from the spike protein of SARS‐CoV‐2 in CHO‐K1 mammalian cells and investigate the binding activity of those proteins with hACE2 receptor, expressed in HEK293T cells using immunofluorescence staining. The plasmids were transiently transfected into the cells, followed by antibiotic selection using G418 as an initial stage to select the positive stable transformants. Protein expression was confirmed by Western blotting and showed an estimated size for monomeric RBD‐fd of 35 kDa and S1‐fd of 55 kDa. However, the trimeric form of the proteins was not observed. In addition, immunofluorescence staining showed the binding activity between the RBD‐fd and S1‐fd proteins and hACE2 expressing cell line, revealing binding and an internalization process.

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  • National Research and Innovation Agency
  • Indonesian Institute of Sciences
  • Bandung Institute of Technology
  • Indonesia International Institute for Life Sciences
  • Universitas Gadjah Mada
  • University of Indonesia
  • Universitas Muhammadiyah Prof Dr Hamka
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Rekan penulisOrganisasiArtikel bersama
Adi SantosoIndonesian Institute of Sciences18
Hariyatun HariyatunIndonesian Institute of Sciences12
Ahmad SuyokoNational Research and Innovation Agency10
Ernawati Arifin Giri-RachmanBandung Institute of Technology10
Fitri Aulia PermatasariBandung Institute of Technology10
Ferry IskandarBandung Institute of Technology10
Marissa AngelinaNational Research and Innovation Agency10
Azzania FibrianiBandung Institute of Technology10
Arizah KusumawatiIndonesian Institute of Sciences7
Khairul AnamNational Research and Innovation Agency7
Neny NurainiPT Bio Farma (Indonesia)5
Ria Fajarwati KastianNational Research and Innovation Agency3
Apon Zaenal MustopaNational Research and Innovation Agency3
Dini NurdianiIndonesian Institute of Sciences2
Edy MeiyantoUniversitas Gadjah Mada2
Rohmad Yudi UtomoUniversitas Gadjah Mada2
Adam HermawanUniversitas Gadjah Mada2
Nuruliawaty UtamiIndonesian Institute of Sciences1
Eko Wahyu PutroIndonesian Institute of Sciences1
Fadlina Chany SaputriUniversity of Indonesia1
Arry YanuarUniversity of Indonesia1
Ni Putu Ermi HikmawantiUniversitas Muhammadiyah Prof Dr Hamka1
Abdul Mun’imUniversity of Indonesia1
Hayati HayatiUniversitas Muhammadiyah Prof Dr Hamka1
Nur Faiizah Aqiilah FirmanAfiliasi tidak diketahui1

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Sumber metadata: OAI-PMH (metadata jurnal) https://jurnal.ugm.ac.id/ijbiotech/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-US">Foldon fusion of RBD and S1 fragments of SARS‐CoV‐2 to stabilize the structure of subunit protein as a vaccine candidate</dc:title>
	<dc:creator>Purwanto, Gracia Christine Lembong</dc:creator>
	<dc:creator>Damai, Fedric Intan</dc:creator>
	<dc:creator>Agustiyanti, Dian Fitria</dc:creator>
	<dc:creator>Wisnuwardhani, Popi Hadi</dc:creator>
	<dc:creator>Fathurahman, Alfi Taufik</dc:creator>
	<dc:creator>Rubiyana, Yana</dc:creator>
	<dc:creator>Ramadani, Ratna Dwi</dc:creator>
	<dc:creator>Sidqi, Muhammad Khairul Lisan</dc:creator>
	<dc:creator>Prasetyaningrum, Pekik Wiji</dc:creator>
	<dc:creator>Septisetyani, Endah Puji</dc:creator>
	<dc:creator>Supriatna, Dadang</dc:creator>
	<dc:creator>Ningrum, Ratih Asmana</dc:creator>
	<dc:creator>Kusharyoto, Wien</dc:creator>
	<dc:creator>Pramanda, Ihsan Tria</dc:creator>
	<dc:creator>Wardiana, Andri</dc:creator>
	<dc:subject xml:lang="en-US">CHO‐K1; Foldon; RBD; SARS‐CoV‐2; Spike</dc:subject>
	<dc:description xml:lang="en-US">The COVID‐19 pandemic threatened public health around the world at the same time as highlighting the urgency of vaccine development. Subunit vaccines are safe and effective vaccine types that utilize parts of viruses to trigger the body’s immune response. Previous research has shown that fusion of the spike protein with the foldon domain (fd) achieved the trimeric form to increase the protein stability of the recombinant subunit protein spike from SARS‐CoV and MERS‐CoV, thus exceeding the immune response in the body. The study aims to observe the expression of RBD‐fd and S1‐fd recombinant proteins from the spike protein of SARS‐CoV‐2 in CHO‐K1 mammalian cells and investigate the binding activity of those proteins with hACE2 receptor, expressed in HEK293T cells using immunofluorescence staining. The plasmids were transiently transfected into the cells, followed by antibiotic selection using G418 as an initial stage to select the positive stable transformants. Protein expression was confirmed by Western blotting and showed an estimated size for monomeric RBD‐fd of 35 kDa and S1‐fd of 55 kDa. However, the trimeric form of the proteins was not observed. In addition, immunofluorescence staining showed the binding activity between the RBD‐fd and S1‐fd proteins and hACE2 expressing cell line, revealing binding and an internalization process.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US">DIPA IPH LIPI 2021</dc:contributor>
	<dc:contributor xml:lang="en-US">RISPRO-LPDP 2020</dc:contributor>
	<dc:date>2023-09-30</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-US">Original Research Articles</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ugm.ac.id/ijbiotech/article/view/82159</dc:identifier>
	<dc:identifier>10.22146/ijbiotech.82159</dc:identifier>
	<dc:source xml:lang="en-US">Indonesian Journal of Biotechnology; Vol 28, No 3 (2023); 173-179</dc:source>
	<dc:source>2089-2241</dc:source>
	<dc:source>0853-8654</dc:source>
	<dc:language>eng</dc:language>
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	<dc:rights xml:lang="en-US">Copyright (c) 2023 The Author(s)</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
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