Research progress in structural proteins of rabies virus
10.3760/cma.j.cn112866-20240401-00052
- VernacularTitle:狂犬病病毒结构蛋白研究进展
- Author:
Minghui ZHANG
1
;
Xiaoyan TAO
;
Wuyang ZHU
Author Information
1. 中国疾病预防控制中心病毒病预防控制所狂犬病室 国家卫健委生物安全重点实验室，北京 102206
- Keywords:
Rabies virus;
Structural protein;
Functional research
- From:
Chinese Journal of Experimental and Clinical Virology
2024;38(5):586-593
- CountryChina
- Language:Chinese
-
Abstract:
Rabies virus (RABV) belonging to the Rhabdoviridae family and the Lyssavirus genus is the main pathogen of rabies and is a single stranded RNA virus with an envelope. The RABV genome encodes five structural proteins: nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and RNA dependent RNA polymerase (RdRp). The N protein mainly plays an important role in the transcription and replication process of viruses, which is often used for diagnosis and virus identification; P protein can interact with some host protein partners, disrupt antiviral signaling pathways, and affect the pathogenicity of RABV; M protein plays an important role in regulating the balance between viral transcription and replication; as a target for inducing neutralizing antibodies, the trimeric structure analysis of G protein before fusion, the influence of fusion rings on successful trimerization and conformational stability, and the visualization of effective and widespread neutralizing antibody epitopes provide a basis for the development of broad-spectrum vaccines. The RdRp protein mainly catalyzes the transcription of viral RNA. In recent years, the analysis of the crystal structure of structural proteins, the discovery of related functional sites, and the interaction with small molecules have helped researchers better understand the pathogenicity of RABV, search for effective antiviral drug targets, and design broad-spectrum vaccines.
