Abstract：Abstract: The 3C-like protease (3CLpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), containing 306 amino acids, is a hydrophilic protease. Its sequence is highly conserved in coronavirus and is critically important for normal function of SARS-CoV-2. To get insight into 3CLpro structure and antigenic epitope positions, series of bioinformatics databases and software were used, and physicochemical property, hydrophobicity, transmembrane region, glycosylation, phosphorylation and sumoylation sites, secondary structure and structural domains, ligand binding sites and potential B/T cell dominant epitopes of the antigen were analyzed. The results showed that 3CLpro contains zero transmembrane region, 2 glycosylation sites, 27 phosphorylation sites, 3 sumoylation sites. Its secondary structure mainly contains α-helices and β-folds. The structural domains also include one endopeptidase/C30 conserved sequence. Moreover, 5 possible ligand binding sites and many epitope regions of B/T cells exist in 3CLpro. Lastly, 8 potential small molecule drugs were detected from DrugBank database. This study may provide a theoretical basis for further research on novel drugs and vaccines against coronavirus disease 2019 (COVID-19).
引用本文:
王 道, 彭 亮. 新型冠状病毒3CL水解酶的结构特征及其抗原表位分析[J]. 生命科学研究, 2020, 24(5): 345-353. WANG Dao, PENG Liang. Analysis of Structural Features and Potential Epitopes in 3C-like Protease (3CLpro) of SARS-CoV-2. Life Science Research, 2020, 24(5): 345-353.
