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    Home > Biochemistry News > Biotechnology News > The electroscopic structure of MERS-CoV and SARS-CoV tri-polymer prick proteins.

    The electroscopic structure of MERS-CoV and SARS-CoV tri-polymer prick proteins.

    • Last Update: 2020-09-07
    • Source: Internet
    • Author: User
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    Recently, Gao Fu, Shi I and Zhang New Deal, researchers of the Institute of Microbiology of the Chinese Academy of Sciences, worked together to analyze the electroscopic structure of THERS-CoV and SARS-CoV trimer pyrethroid proteins (Spike glycoprotein, S) with near-atomic resolution. Compared with other previously published coronavirus S proteins, they found that these two highly pathogenic viruses have free receptor binding regions, which are more beneficial to the binding of S proteins and host receptors, and provide a critical three-dimensional structural map for subsequent broad-spectrum antibodies and vaccine design.
    results were published online April 10 in Nature Communications.
    Middle East Respiratory Syndrome (MERS-CoV) is another highly pathogenic coronavirus (SARS-CoV) that has emerged after severe acute respiratory syndrome (SARS-CoV), which has spread to many countries and regions around the world and become another serious challenge to the world's public health security.
    virus intrusion into the host begins with the interaction between the viral surface protein and the host cell surface-specific complex.
    In MERS-CoV and SARS-CoV, the prickly protein on the viral cystic membrane is responsible for binding the subject, determining the virus's ability to invade the host and tissue specificity, and is an important target for the development of drugs or vaccines to prevent and treat coronavirus-related diseases.
    researchers used single-particle cryoscopic technology to analyze the pre-fusion structure of the near-atomic resolution MERS-CoV and SARS-CoV trimer S proteins at resolutions of 3.7 and 3.2 , respectively.
    the overall structure of these two highly pathogenic coronavirus trijustular S proteins is similar to that of reported coronavirus, but their subject binding region (RBD) differs significantly from other coronavirus.
    researchers captured RBDs in both MERS-CoV and SARS-CoV states, one buried (i.e., horizontal, lying state) and the other exposed (i.e., standing state, state standing).
    reported coronavirus RBDs are almost all enculated, while both MERS-CoV and SARS-CoV are exposed, a state in which RBD facilitates the binding of receptors and provides a theoretical basis for the clarification of the binding mechanism between viruses and cell surface receptors.
    1: MERS-CoV and SARS-CoV S trimer-binding model diagram.
    (a) MERS-CoV S trimer and subject CD26, (b) SARS-CoV S trimer and subject ACE2.
    2: N-connected glycosylation analysis of MERS-CoV and SARS-CoV S proteins and possible antiviral strategies for human coronavirus.
    (a) N-connection glycosylation of MERS-CoV S protein, (b) N-connecting glycosylation of SARS-CoV S protein, (e-f) conservative analysis of human coronavirus sequences.
    , the researchers used X-ray crystallology to analyze the structure of MERS-NTD and SARS-NTD for the first time.
    N-terminal domain (N-terminal domain, NTD) of the S protein can bind to sugar or subject molecules in some coronavirus, helping the virus to adhere to and invade host cells.
    but the structure and function of MERS-NTD and SARS-NTD were previously unclear.
    study found that the unique sugar binding regions of the two viruses, NTD, determined that they could not bind sugar molecules like some coronavirus NTDs to complete the virus's adhesion to cells.
    addition, the NTD and RBD of the S protein are structurally adjacent, so NTD also has the potential to act as a neutral antibody target.
    's conservative analysis of the six coronavirus sequences of infected people found that fusion peptides, hepteptide repeat zone 1 (HR1) and central helix as relatively conservative and easily accessible areas were ideal for finding and developing broad-spectrum neutral antibodies and inhibitors.
    analysis of the structure of the full-length S protein trimer is of great theoretical significance for the understanding of the pathogenic mechanisms of MERS-CoV and SARS-CoV, as well as for the development of specific drugs and the practice of vaccine design in the process of targeting virus invasion.
    The University of Science and Technology of China and the Institute of Microbiology of the Chinese Academy of Sciences jointly trained Ph.D. student Yuan Yuan, Ph.D. Cao Endfang of the Institute of Biophysics, Ph.D. graduate student of the Institute of Microbiology, Zhang Yanfang, Assistant Researcher of Tianjin Institute of Industrial Biotechnology, and Ma Jun, Ph.D., Institute of Biophysics, as co-authors of the paper.
    Gaofu, Shi I and Zhang New Deal are co-authors of the thesis.
    The study was supported by the Strategic Pilot Project of the Chinese Academy of Sciences, the National "973" Program, the National Natural Science Foundation of China's Excellent Youth Fund, the Youth 1,000 Program of the Central Group Department, and the National Key Research and Development Program.
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