Reporters learned from the University of Science and Technology of China, the university’s School of Life Sciences Professor Bi Guoqiang team and peer cooperation, the use of high-resolution frozen electro-mirror single-particle analysis technology for the first time to analyze the human herpes virus type 6B near atomic resolution structure. The results of the study have been published online in the internationally renowned journal Nature Communications.
CryoEM imaging technology analyzes the 3D structure of HHV-6B virus and pU11 tetrapolymers
Human herpes virus type 6 (HHV-6) belongs to the herpes virus family beta herpes virus subfamily, according to its surface antigen, but also divided into HHV-6A and HHV-6B two closely related virus types. Many young children are infected with HHV-6 virus, and may produce fever, diarrhea, red rash and other clinical symptoms, HHV-6 virus can lurk in the human body for life, and in people with low immunity causeserious disease, it in the brain tissue secondary outbreak will lead to cognitive disorders, disability or death. Studies have shown that the HHV-6 virus is even linked to Alzheimer’s disease and epilepsy. HHV-6 virus infection causes widespread harm, but there is currently no high resolution structure for the virus, as well as structural-based drugs or vaccine antiviral programs. Because of its high bonding with the host cell, HHV-6B is difficult to realize in vitro proliferation culture, which becomes a difficult problem in the analysis of its atomic resolution structure.
Using advanced cryoscope direct electron counting technology and subparticle local reconstruction method, the researchers analyzed the first near atomic resolution structure of HHV-6B with a small number of low-purity Samples of HHV-6B virus. On this basis, the team built an atomic model of the HHV-6B virus 4 kinds of shell protein and 1 type of shell binding interlayer protein pU11, including a total of 59 conformations. Further, by comparing the similarities and differences between HHV-6B, human cytomegalovirus and mouse cytomegalovirus nuclear crust structure, it is found that HHV-6B interlayer protein pU11 has a unique virus crust binding pattern.
The findings reveal at the atomic level the mechanism by which compounds in different herpes viruses assist the virus’s crust to cope with the internal pressures generated by different genome sizes. It helps to better understand the packaging of the beta herpes virus genome and the stabilization mechanism of the virus’s nuclear crust, improves the understanding of the family structure of the herpes virus, enriches and deepens the understanding of the functional mechanism of the beta herpes virus virus and even the whole herpes virus family complex.