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

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 immuno-genicity. 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.