Identification of Compounds Targeting Hepatitis B Virus Core Protein Dimerization through a Split Luciferase Complementation Assay

• DOI: 10.1128/aac.01302-18
• Publication Date: 2018-09-17T14:07:52Z
• Authors: Xia-Fei Wei; Chun-Yang Gan; Jing Cui; Ying-Ying Luo; Xue-Fei Cai; Yi Yuan; Jing Shen; Zhi-Ying Li; Wen-Lu Zhang; Quan-Xin Long; Yuan Hu; Juan Chen; Ni Tang; Haitao Guo; Ai-Long Huang; Jie-Li Hu
• Keywords: DNA Replication; Gene Expression Regulation, Viral; 0301 basic medicine; Hepatitis B virus; Indoles; Core protein; Split luciferase; Recombinant Fusion Proteins; Antiviral Agents; Cell Line; 03 medical and health sciences; Capsid; Genes, Reporter; Humans; Luciferases; 20-deoxyingenol; Arbidol; Viral Core Proteins; High-Throughput Screening Assays; 3. Good health; Dimer; HEK293 Cells; Cell model; Compound screen; DNA, Viral; Hepatocytes; Diterpenes; Protein Multimerization; Protein Binding

The capsid of the hepatitis B virus is an attractive antiviral target for developing therapies against chronic hepatitis B infection. Currently available core protein allosteric modulators (CpAMs) mainly affect one of the two major types of protein-protein interactions involved in the process of capsid assembly, namely, the interaction between the core dimers.