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    Home > Biochemistry News > Microbiology News > Gaofu team, first article in 2023

    Gaofu team, first article in 2023

    • Last Update: 2023-02-02
    • Source: Internet
    • Author: User
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    On January 5, 2023, Gao Fu, Wang Qihui and Qi Jianxun of the Institute of Microbiology, Chinese Academy of Sciences jointly published a title online in the EMBO Journal (IF=14).
    "Host range and structural analysis of bat-origin RshSTT182/200 coronavirus binding to human ACE2 and its animal orthologs", the study The structure of the RshSTT182/200 receptor-binding domain (RBD) and human angiotensin-converting enzyme 2 (hACE2) complexes was determined, and key residues
    affecting receptor binding were identified.
    The study combined RshSTT182/200 RBD with ACE2 orthologs from 39 animals, including 18 species of bats, and has assessed its host range

    RshSTT182/200 RBD broadly identified 21 of the 39 ACE2 orthogenes, although its binding affinity with the orthocompounds was weaker than that of SARS-CoV-2 RBD
    In addition, the RshSTT182 pseudovirus can enter cells
    using the ACE2 receptors of humans, foxes, and nasal frogs.
    The researchers also found that SARS-CoV-2 induced cross-neutralizing antibodies
    against the RshSTT182 pseudovirus.
    Taken together, these findings suggest that RshSTT182/200 may infect susceptible animals, but further evolution is needed to acquire a capacity for interspecific transmission as strong as SARS-CoV-2

    Seven coronaviruses have been reported to infect humans, including severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), human coronavirus NL63 (HCoV-NL63), human coronavirus OC43 (HCoV-OC43), human coronavirus 229E ( HCoV-229E), human coronavirus HKU1 (HCoV-HKU1) and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).

    In the last 20 years, three public health emergencies have been caused by coronaviruses:
    the SARS-CoV pandemic (2002), the MERS-CoV pandemic (2012), and the SARS-CoV-2 pandemic (2019).

    For many viral infectious diseases, the discovery of viruses often lags by decades or more
    For example, HCoV-HKU1 was first detected
    in 2004 in a patient with pneumonia in Hong Kong, China.
    However, a frozen nasopharyngeal swab sample from a Brazilian child in 1995 tested positive for HCoV-HKU1, indicating that HCoV-HKU1 had been circulating in the population for a long time
    MERS-CoV was first detected in Saudi Arabia in 2012, while 81% of dromedary serum samples collected in Egypt in 1997 and in Sudan and Somalia in 1983-1984 were positive
    for MERS-CoV neutralizing antibodies.
    Therefore, assessing potential interspecific transmission of the virus is an effective way
    to raise infectious disease alert as early as possible.
    Bats are thought to host
    HCoV-NL63, HCoV-229E, SARS-CoV, and MERS-CoV.
    At the beginning of the SARS-CoV-2 pandemic, several SARS-CoV-2-related coronaviruses
    were detected in bats.
    The overall genome of bat-derived coronavirus RaTG13 is 96.
    identical to the nucleic acid sequence of SARS-CoV-2.
    Another coronavirus derived from bats, RmYN02, contains a 3-amino acid residue (PAA) insertion site at the S1/S2 cleavage site of its spike protein, which is similar to SARS-CoV-2, while this has not been observed in other SARS-CoV-2-related coronaviruses

    The furin protease cleavage site (FCS) plays a key role in SARS-CoV-2 infection, and the absence of this site reduces viral entry efficiency
    Recently, several bat-source CoVs, BANAL-52, BANAL-103 and BANAL-236
    , have been identified in bat bodies in northern Laos.
    The receptor-binding domains (RBDs) of the spike proteins of BANAL-52, BANAL-103, and BANAL-236 are 95% identical to those of SARS-CoV-2 and exhibit similar binding affinities to SARS-CoV-2 RBD and hACE2, suggesting that these viruses may infect humans
    。 RshSTT182 and RshSTT200 are the first SARS-CoV-2-associated coronaviruses detected in Southeast Asia (Cambodia) with a genome-wide homology of 92.
    with SARS-CoV-2.
    RshSTT182 and RshSTT200 RBD have the same amino acid sequence and have 84.
    3% homology with SARS-CoV-2 RBD
    Interspecific receptor recognition by SARS-CoV, SARS-CoV-2, RaTG13, GX/P2V/2017, and GD/1/2019 has been
    All of these coronaviruses widely identify different ACE2 congeners, suggesting that they may be circulating
    between different animals.
    In addition, several cases
    of natural infection with SARS-CoV-2 have been reported.
    Cats, dogs, lions and tigers in zoos, as well as mink, ferrets, snow leopards, cougars and gorillas in nature, have been found to have contracted SARS-CoV-2
    through exposure to people with COVID-19.
    In addition, the SARS-CoV-2 strain associated with mink has spread back to humans and caused further community transmission
    The overall structure of RshSTT182/200 RBD binding to hACE2 (Figure from EMBO Journal) It is worth noting that SARS-CoV-2 variants were detected in infected mink, suggesting that interspecific transmission may produce new variants
    RshSTT182/200 RBD is highly conserved with SARS-CoV-2 RBD and may also have a wide host range
    Host cell receptor binding is a prerequisite for
    viral infection.
    Therefore, describing the interaction between RBD of CoV and ACE2 orthologs from a wide range of species is an effective method
    to screen potential hosts.
    Receptor binding is the first step
    in coronavirus infection.
    A range of protein and carbohydrate receptors/cofactors have been identified
    ACE2 is the main receptor for SARS-CoV, SARS-CoV-2 and its related coV, such as RaTG13, GX/P2V/2017, GD/1/2019
    The structure of SARS-CoV-2 RBD complexes with ACE2s complexes in humans, cats, bats, dogs, martens and pangolins has been determined
    In addition, the structure of hACE2 binding to RaTG13, GX/P2V/2017 and GD/1/2019 RBDs has been studied
    GX/P2V/2017 RBD and GD/1/2019 RBD utilize similar binding mechanisms to SARS-CoV-2 and show similar binding affinity
    to hACE2 with SARS-CoV-2 RBD.
    Similar to other CoVs associated with SARS-CoV-2, RshSTT182/200 also uses ACE2 as its receptor.

    However, the molecular details of RshSTT182/200 RBD binding to ACE2 are unknown
    In this study, the researchers found that RshSTT182/200 RBD has a much lower binding affinity for hACE2 than SARS-CoV-2 RBD
    They determined the structure of the RshSTT182/200 RBD with hACE2 complexes and identified key residues
    As a kind of batThe receptor binding spectrum of the source coronavirus, RshSTT182/200, in 18 species of bats is narrower
    than that of SARS-CoV-2.
    In addition, the study evaluated the receptor binding profile
    of RshSTT182/200 RBD with 21 animal ACE2 homologous sequences, including hACE2.
    RshSTT182/200 RBD extensively identified 16 of the 21 ACE2 orthogenites with significantly lower binding affinity than SARS-CoV-2
    ACE2 receptors in humans, foxes, and R.
    affinis support VSV-based RshSTT182 pseudoviral transduction, but hACE2-mediated entry is less efficient
    In addition, serum of SARS-CoV-2 convalescent patients or vaccinated patients can cross-neutralize VSV-based RshSTT182 pseudovirus, and SARS-CoV-2 monoclonal antibodies S309, BD-368-2, and BD-604 can cross-identify RshSTT182/200 RBD
    These results suggest that
    surveillance of RshSTT182/200 and its associated coronaviruses carried by potential animal reservoirs should be intensified to prevent potential pandemics

    Paper information: https://doi.
    2022111737 Source:
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