Crystal structure of EV71 mature virus particles and empty virus particles
On March 4, the international academic journal Nature-Structure and Molecular Biology published the latest research results of hand-foot-mouth virus EV71 by Rao Zi and the research group of the Institute of Biophysics, Chinese Academy of Sciences (DOI: doi: 10.1038 / nsmb.2255 ).
In March 2008, a serious HFMD epidemic occurred in Fuyang City, Anhui Province. In just two months, there were more than 3,700 cases of HFMD in Fuyang City, and 22 people died, causing a whole society. s concern. The outbreak was soon confirmed as an enterovirus EV71 infection. In May 2008, the Ministry of Health quickly included hand-foot-mouth disease as a Category C infectious disease in China for management. As of today, in less than 4 years, there have been more than 4 million new cases in the country, resulting in nearly 2,000 deaths, most of them children under 5 years old. The prevalence of hand-foot-mouth disease poses a huge threat to China's public health security, and due to the lack of vaccines and special drugs against the EV71 virus, this threat continues to this day.
The research team led by Academician Rao Zihe cooperated with Professor Wang Junzhi's research group of China National Institute for the Control of Pharmaceutical and Biological Products and Professor Stuart's research group of Oxford University in the UK to complete virus culture purification, high-quality crystal growth, diffraction data collection and structural analysis After a series of key steps, the high-resolution crystal structures of two distinct virus particles of EV71 virus were successfully analyzed. This is the first time that a high-resolution three-dimensional structure of the hand-foot-mouth disease virus EV71 has been obtained worldwide, and it is also the first time that two high-resolution three-dimensional structures of the same virus have been obtained at the same time. Among them, the diameter of EV71 whole virus particles reached 340 Angstroms, the entire capsid was composed of 240 protein subunits, about 408,000 atoms (excluding hydrogen atoms), and the total molecular weight reached 5.7 million Daltons. The largest compound structure resolved.
During the initial purification and detection of EV71 virus obtained in vitro, the research team found two types of EV71 virus particles with very different properties. One of them is normal and contains whole virus particles with a complete genome. The other is a hollow virus particle that does not contain a genome and has a slightly expanded volume. This unexpected discovery aroused the strong interest of the research team members. After a carefully designed experiment, the researchers separated the two particles, cultivated them separately, and finally analyzed the high-resolution crystal structures of the two EV71 virus particles.
Through careful analysis of the structure of the entire EV71 virus particle, the researchers identified the area where the EV71 virus interacts with host cell receptors, and identified potential epitopes of the EV71 virus. These findings will provide a solid structural basis for the development of highly effective vaccines against the EV71 virus and specific therapeutic antibodies.
In addition, by comparing the structure of the two virus particles, the researchers also found that 90 hollow holes were regularly distributed on the surface of the hollow virus particles. From this, the researchers speculate that these holes can be used as a channel for RNA genome export during virus decapsulation. Decapsulation is a necessary step for viruses to infect the host. Previous studies have shown that enteroviruses, after adhering to the host cell surface, will be endocytosed into the host cell to form endosomes. In the endosome, the virus completes the decapsulation process, releasing the RNA genome wrapped by the capsid into the host cell. The decapsulation process of enteroviruses is critical to its infection of the host, but its detailed mechanism is still unknown. Although there are various speculations about this process by the academic community, there are many possible mechanisms, but because of the lack of key structural information, no mechanism can be widely recognized. The huge holes on the surface of the EV71 hollow virus particles observed this time led the researchers to propose a new and convincing mechanism for enterovirus decapsulation.
In addition, the researchers found that a conserved hydrophobic pocket in the EV71 viral capsid protein VP1 may be a potential drug binding target. Through the targeted design of small molecule inhibitors, the conformational change of the hydrophobic pocket can be suppressed, so as to inhibit the uncoating process of EV71 virus, block the replication of EV71 virus in the human body, and finally treat hand, foot and mouth disease caused by EV71 virus infection the goal of.
The acquisition of these results provides a solid foundation for a deeper understanding of the pathogenic mechanism of EV71 virus and the development of targeted prevention and treatment methods. At present, Rao Zihe and his research team are further developing vaccines, therapeutic antibodies and small molecule inhibitors for EV71 virus on this basis, striving to make more efforts to overcome hand-foot-mouth disease, a major disease that seriously threatens China's public health and safety Great contribution.
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