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    Home > Active Ingredient News > Infection > Nat Commun: The reason why the new crown virus is hard to beat has been found! It turns out to mimic the human mRNA "hat structure"

    Nat Commun: The reason why the new crown virus is hard to beat has been found! It turns out to mimic the human mRNA "hat structure"

    • Last Update: 2020-08-05
    • Source: Internet
    • Author: User
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    The "raid" of SARS-CoV-2 has set off a "bloody rain" around the world, which lasted six months, to the relief and pride of the nation, that China's new crown epidemic has been better controlled.
    However, why is this "toss" global restless virus so hard to eliminate? Recently, Nature Communication published an article entitled "R.R.I.A. by SARS-CoV-2", which answered our questions.
    the study found that SARS-CoV-2 was able to simulate a person's mRNA modification process to "disguise" itself, thus smoothly escaping the recognition of the immune system.
    the study revealed the specific mechanism of the SARS-CoV-2 virus mRNA cap closure and found antiviral sites that could be used for treatment, providing a novel solution for the treatment of neo-coronapneumonia (COVID-19).
    previous studies have shown that SARS-CoV-2 replicates and transcribes its RNA through membrane binding enzyme complexes of a variety of viral non-structural proteins.
    in the RNA synthesis process, in order to "disguise" the structure of eukaryotic mRNAs, SARS-CoV-2 will be "capped" from the first nucleotide of S-adenosine thionine (SAM) methylation mRNA 2'-O, the 5' end of the viral mRNA, to complete the transformation from RNA "cap 0" (Cap-0, me7GopppA1) to "Cap 1" (Cap1) the activity of
    nsp16 and nsp10 (non-structural proteins) can affect the "cap modification" process of SARS-CoV-2.
    nsp16 needs to be combined with nsp10 to play the function of methyl transferase, the formation of nsp16/nsp10 complex for the synthesis and stability of viral RNA and the proliferation of viruses play an important role.
    in this study, the researchers successfully observed the high-resolution structureof (resolution up to 1.8?) of the SARS-CoV-2nsp16 and nsp10 triaves in the presence of the homogenous RNA substrate analogues and methyl donor SAM. )。
    , they found that nsp16/nsp10 isopolymers were formed by methylated SARS-CoV-2mRNA's first nucleotide nucleosacin 2'-O.
    researchers also compared the structure of ribose 2'-O of dengue virus (PDBID:5DT0) and bovine pox (PDBID:1AV6) and found that the geometric arrangement of RNA caps in RNA/DNA viruses was different, and speculated that specific anti-SARS-CoV-2 virus escants could be designed using the special structure of SARS-CoV-2RNA caps.
    next, in order to better understand the role of acquired mutations in SARS-CoV-2nsp16, the researchers compared the nsp16 sequences of three subspecies (alpha, beta, and gamma) coronavirus strains, and interestingly, the mutations present in SARS-CoV-2nsp16 had a high degree of similarity to those related to the NEW York City outbreak of COVID-19. in addition
    , they have made a major discovery: the presence of other alternative ligand binding sites in nsp16 that can be used to bind small molecules. what does
    mean? Simply put, scientists are hoping to develop small molecular drugs that inhibit nsp16 from forming complexes, blocking the "cap-and-cap" process of SARS-CoV-2, in which the body's immune system can recognize the SARS-CoV-2 virus and prevent the body from being attacked by the virus.
    in summary, the study revealed the 3D structure of a key enzyme needed in the replication of the SARS-CoV-2 virus, and also found binding sites in this structure that inhibit the key enzyme.
    imagine, perhaps we could design drugs that target SARS-CoV-2 and emerging coronaviruses through the alternative junctionofs of nsp16.
    this will be another significant step forward on the basis of our existing understanding of the virus.
    .
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