Liu Liqing, Chen Hong, Liu Ping, Ke Xiongfeng, Song Jingjing, Fang Ying, Kong Lingbao, Xin Xiu
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.
Vet Res Forum. 2024;15(12):657-663. doi: 10.30466/vrf.2024.2013858.4037. Epub 2024 Dec 15.
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 gene was inserted into pET-28a vector, and efficiently expressed in 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.
严重急性呼吸综合征冠状病毒2(SARS-CoV-2)引发了新冠疫情。位于SARS-CoV-2刺突蛋白上的受体结合域(RBD)在病毒感染期间包含大多数中和表位,是疫苗开发的理想抗原。在本研究中,对SARS-CoV-2 RBD蛋白的氨基酸序列数据进行了生物信息学分析,以更好地了解其分子特征。该基因被插入到pET-28a载体中,并在 系统中高效表达。然后,纯化重组蛋白(RBD单体和RBD二聚体蛋白)作为动物免疫的抗原。此外,结果表明重组蛋白(RBD单体和RBD二聚体蛋白)具有足够的免疫原性,可刺激免疫小鼠产生针对相应蛋白的特异性抗体。综上所述,本研究结果表明RBD蛋白具有高免疫原性。本研究可能对SARS-CoV-2检测的未来发展具有启示意义。