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作 者:Na Li Zhiqiang Li Yan Fu Sheng Cao
机构地区:[1]CAS Key Laboratory of Special Pathogens and Biosafety,Wuhan Institute of Virology,Wuhan 430071,China [2]Center for Biosafety Mega-Science,Chinese Academy of Sciences,Wuhan 430071,China [3]University of Chinese Academy of Sciences,Beijing 100049,China
出 处:《Virologica Sinica》2020年第1期1-13,共13页中国病毒学(英文版)
基 金:the National Natural Science Foundation of China(Grant Nos.31570161 and 31770169);the“One-Three-Five”Strategic Programs of the Wuhan Institute of Virology,Chinese Academy of Sciences(Grant No.Y605211SA3).
摘 要:Antibodies play critical roles in neutralizing viral infections and are increasingly used as therapeutic drugs and diagnostic tools. Structural studies on virus-antibody immune complexes are important for better understanding the molecular mechanisms of antibody-mediated neutralization and also provide valuable information for structure-based vaccine design.Cryo-electron microscopy(cryo-EM) has recently matured as a powerful structural technique for studying bio-macromolecular complexes. When combined with X-ray crystallography, cryo-EM provides a routine approach for structurally characterizing the immune complexes formed between icosahedral viruses and their antibodies. In this review, recent advances in the structural understanding of virus-antibody interactions are outlined for whole virions with icosahedral T = pseudo 3(picornaviruses) and T = 3(flaviviruses) architectures, focusing on the dynamic nature of viral shells in different functional states. Glycoprotein complexes from pleomorphic enveloped viruses are also discussed as immune complex antigens. Improving our understanding of viral epitope structures using virus-based platforms would provide a fundamental road map for future vaccine development.
关 键 词:Cryo-electron microscopy(Cryo-EM) ICOSAHEDRAL ANTIGEN VIRION IMMUNE complex
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