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    Home > Active Ingredient News > Immunology News > Immunity Tsinghua University and other institutions cooperated, Zhang Linqi/Wang Xinquan/Zhang Tong systematically analyzed the new coronavirus variants and revealed the neutralization escape mechanism

    Immunity Tsinghua University and other institutions cooperated, Zhang Linqi/Wang Xinquan/Zhang Tong systematically analyzed the new coronavirus variants and revealed the neutralization escape mechanism

    • Last Update: 2021-06-17
    • Source: Internet
    • Author: User
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    Editor’s note iNature is China’s largest academic official account.
    It is jointly created by the doctoral team of Tsinghua University, Harvard University, Chinese Academy of Sciences and other units.
    The iNature Talent Official Account is now launched, focusing on talent recruitment, academic progress, scientific research information, interested parties can Long press or scan the QR code below to follow us
    .

    The iNatureSARS-CoV-2 variant continues to appear during the global pandemic and may help evade current antibody therapy and vaccine protection
    .

    On June 8, 2021, Tsinghua University, Capital Medical University and other organizations cooperated.
    Zhang Linqi, Wang Xinquan, Zhang Tong and Joint Communication published an online publication titled "Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability" in Immunity.
    to use ACE2 receptors from additional species", the study found that the South African variant B.
    1.
    351 is the most resistant to monoclonal antibodies and convalescent plasma from people infected with COVID-19, followed by the Brazilian variant P.
    1 and British variant B.
    1.
    1.
    7
    .

    This resistance level corresponds to the Y144del and 242-244del mutations in the N-terminal domain of SARS-CoV-2 and the K417N/T, E484K and N501Y mutations in the receptor binding domain (RBD)
    .

    B.
    1.
    351 Triple mutant (417N-484K-501Y) RBD and monoclonal antibody P2C-1F11 complex crystal structure analysis reveals the molecular basis of antibody neutralization and escape
    .

    B.
    1.
    351 and P.
    1 also gained the ability to use mouse and mink ACE2 receptors to enter
    .

    The results show that the main antigenic shift and potential expansion of the host range of B.
    1.
    351 and P.
    1 variants pose a serious challenge to current antibody therapy and vaccine protection
    .

    The current neutralizing antibody and vaccine strategy against SARS-CoV-2 (the causative agent of COVID-19) is adopted in the early stages of the pandemic
    .

    Some regulatory agencies have recently approved these antibody and vaccine options for emergency use authorization (EUA), and will begin rolling out to high-risk groups at the end of 2020
    .

    Eli Lilly and Regeneron have developed monoclonal neutralizing antibodies against the receptor binding domain, which have been shown to reduce patient viral load and COVID-19-related symptoms and hospitalization rates
    .

    Hundreds of RBD-specific mAbs have been isolated and characterized from SARS-CoV-2 infected patients, some of which are in active clinical development
    .

     Pfizer/BioNtech and Moderna developed an mRNA vaccine expressing a stable form of S protein, which proved to be 95% effective against symptomatic infections and reduced the risk of serious diseases
    .

    Other vaccine methods, such as adenovirus-based, protein subunits, and inactivated vaccines, have also proven to be quite effective
    .

    However, there is growing concern that the global pandemic may produce new SARS-CoV-2 variants that are antigenically different from the prototype strain, thus rendering current antibody and vaccine strategies ineffective
    .

    As of May 17, 2021, about 1,200,000 SARS-CoV-2 genome sequences have been included in the GISAID database, and at least more than 6,200 amino acid substitutions, deletions and insertions have been found in the S protein
    .

    Of the latter, 1818 are located in the N-terminal domain (NTD), 968 are located in the RBD, 741 are located in subdomains 1 and 2 (SD1-2), and 2481 are located in the S2 region
    .

    Article pattern (picture from Immunity) Although these mutations are driven by the inherent and error-prone nature of the RNA-dependent RNA polymerase (RdRp) encoded by the virus, their survival and maintenance depend on natural infection, transmission and host Selective advantages in the process of adaptation
    .

    For example, the S protein D614G mutation predominates only a few months after the pandemic, and is associated with greater infectivity and a moderate reduction in sensitivity to antibody neutralization
    .

    However, the recently discovered SARS-CoV-2 variants (B.
    1.
    1.
    7 in the United Kingdom, B.
    1.
    351 in South Africa and P.
    1 in Brazil) have attracted strong attention
    .

    Not only did they quickly replace the local SARS-CoV-2 strain, but they also carry NTD and RBD mutations that are essential for interaction with ACE2 receptors and neutralizing antibodies, specifically, B.
    1.
    1.
    7, B.
    1.
    1.
    7, B.
    1.
    351 and P.
    1 share the previously shown N501Y mutation (which enhances the binding affinity to ACE2)
    .

    B.
    1.
    351 and P.
    1 have three common mutation sites in RBD-K417N/T, E484K and N501Y, which may change their antigen profile
    .

    In addition, various deletion mutants were found in NTD, such as 69-70del and Y144del in B.
    1.
    1.
    7, and 242-244del in B.
    1.
    351
    .

    Some mutations were also found in the SD1-2 region near the furin cleavage site, such as P681H in B.
    1.
    1.
    7 and A701V in B.
    1.
    351
    .

    Since all these mutations are located at or near the main S protein antigenic site, they may adversely affect the neutralization of antibodies induced by natural infection or vaccination
    .

    The study found that the South African variant B.
    1.
    351 has the strongest resistance to monoclonal antibodies and convalescent plasma from people infected with COVID-19, followed by the Brazilian variant P.
    1 and the British variant B.
    1.
    1.
    7
    .

    This resistance level corresponds to the Y144del and 242-244del mutations in the N-terminal domain of SARS-CoV-2 and the K417N/T, E484K and N501Y mutations in the receptor binding domain (RBD)
    .

    B.
    1.
    351 Triple mutant (417N-484K-501Y) RBD and monoclonal antibody P2C-1F11 complex crystal structure analysis reveals the molecular basis of antibody neutralization and escape
    .

    B.
    1.
    351 and P.
    1 also gained the ability to use mouse and mink ACE2 receptors to enter
    .

    The results show that the main antigenic shift and potential expansion of the host range of B.
    1.
    351 and P.
    1 variants pose a serious challenge to current antibody therapy and vaccine protection
    .

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