Veterinary Research Forum
Vet Res Forum

Expression, purification and immunogenicity analyses of receptor binding domain protein of severe acute respiratory syndrome coronavirus 2 from delta variant

Document Type : Original Article

Authors

Liqing Liu
Hong Chen
Ping Liu
Xiongfeng Ke
Jingjing Song
Ying Fang
Lingbao Kong
Xiu Xin

Institute of Pathogenic Microbiology, College of Biological Science and Engineering, and Nanchang Key Laboratory of Animal Virus and Genetic Engineering, Jiangxi Agricultural University, Nanchang, China

https://doi.org/10.30466/vrf.2024.2013858.4037
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the COVID-19 pandemic. The receptor binding domain (RBD), located at the spike protein of SARS-CoV-2, contains most of the neutralizing epitopes during viral infection and is an ideal antigen for vaccine development. In this study, bioinformatic analysis of the amino acid sequence data of SARS-CoV-2 RBD protein for the better understanding of molecular characteristics was performed. The SARS-CoV-2 RBD gene was inserted into pET-28a vector, and efficiently expressed in E. coli system. Then, the recombinant proteins (RBD monomer and RBD dimer protein) were purified as antigen for animal immunization. Furthermore, the results showed that the recombinant proteins (RBD monomer and RBD dimer protein) had adequate immunogenicity to stimulate specific antibodies against the corresponding protein in immunized mice. Taken together, the results of this study revealed that RBD protein had a high immunogenicity. This study might have implications for future development of SARS-CoV-2 detection.

Keywords

Delta mutant of SARS-CoV-2
Immunogenicity research
Prokaryotic expression
Receptor binding domain

Subjects

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Veterinary Research Forum
Volume 15, Issue 12
December 2024
Pages 657-663

  • Receive Date 19 October 2023
  • Revise Date 03 January 2024
  • Accept Date 05 February 2024

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