新冠病毒受体结合域与人血管紧张素转换酶2结合力研究进展  

Research Progress on the Binding Affinity between the SARS-CoV-2 Receptor-Binding Domain and Human Angiotensin-Converting Enzyme 2

作　　者：曾嘉锋 续芮 陈操[1] ZENG Jiafeng;XU Rui;CHEN Cao(National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases,NHC Key Laboratory of Medical Virology and Viral Diseases,National Institute for Viral Disease Control and Prevention,Chinese Center for Disease Control and Prevention,Beijing 102206,China)

机构地区：[1]传染病溯源预警与智能决策全国重点实验室,国家卫生健康委员会医学病毒与病毒病重点实验室,中国疾病预防控制中心病毒病预防控制所,北京102206

出　　处：《病毒学报》2025年第1期193-201,共9页Chinese Journal of Virology

基　　金：国家重点研发计划(项目号:2023YFC2306000);国家自然科学基金(项目号:82341035,82341034);新冠病毒变异株风险研判及数据共享研究(项目号:GJJKJ-2023)。

摘　　要：新冠病毒通过其刺突蛋白的受体结合域与人细胞血管紧张素转换酶2结合是病毒感染的重要环节。本文围绕新冠病毒刺突蛋白的受体结合域,分析了五种关注变异株的刺突蛋白受体结合域氨基酸突变对与血管紧张素转换酶2结合力的影响,探讨了新冠病毒与血管紧张素转换酶2结合的主要机制,以及受体结合域突变对“病毒-宿主”结合的影响。总结了病毒与受体结合力的传统与新兴研究方法,如生物化学、晶体学等。这些技术有助于更好地理解病毒的入侵机制,预测病毒变异的传播趋势和防控策略,最终为防控新冠疫情提供科学依据。The binding of the SARS-CoV-2 spike protein's receptor-binding domain(RBD)to human angiotensin-converting enzyme 2(ACE2)is a critical step in the viral infection process.This review focuses on the SARS-CoV-2 spike protein RBD,examining how amino acid mutations in the RBD of five variants of concern affect their binding affinity to ACE2.It further explores the primary mechanisms underlying the interaction between SARS-CoV-2 and ACE2,as well as the impact of RBD mutations on virus-host binding.In addition,this review summarizes both traditional and emerging methodologies used to study virus-receptor binding affinity,including biochemical techniques and crystallography.These approaches contribute to a more comprehensive understanding of viral entry mechanisms,support the prediction of transmission trends in viral variants,and inform effective prevention and control strategies,thereby providing a scientific basis for mitigating the COVID-19 pandemic.

关 键 词：新冠病毒 受体结合域 血管紧张素转换酶2 受体 结合力 

分 类 号：R373.1[医药卫生—病原生物学]