echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Medical News > Latest Medical News > The structure of hedgehog glycoprotein reveals new clues to the natural evolution of the new coronavirus

    The structure of hedgehog glycoprotein reveals new clues to the natural evolution of the new coronavirus

    • Last Update: 2020-11-29
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com

    BEIJING, July 13 (Xinhua Zhang Mengran) According to a recent paper published in the British journal Nature Structure and Molecular Biology, the Francis Crick Institute in the United Kingdom has made a new achievement: a sign of the new coronavirus and its near-bat virus RaTG13's hedgehog glycoprotein structure - prickly glycoprotein can allow the virus to bind to cells and enter the cells. This structure provides information for further understanding the evolution of the new coronavirus protrusion, and is of great significance to vaccine design.
    researchers believe the bat coronavirus may be an evolutionary premed for the new coronavirus, after previous studies found that the close relationship between the bat virus RaTG13 and the new coronavirus is the closest known. However, there is a 3.8% difference between the genome sequences of the new coronavirus and RaTG13, which means that there are nearly 1,100 nucleotide differences between the two.
    Trevor Bedford, a bioinfractics expert at the University of Washington in Seattle, USA, has combined differences in nucleotides between viruses with other hypothetical mutation rates of coronavirus, arguing that the two viruses share a common ancestor between 25 and 65 years ago, and that ratG13-like viruses can take at least a few decades to mutate into new coronavirus.
    Anthony Worobel, Donald Benton and colleagues at the Francis Crick Institute in the United Kingdom compared the new coronavirus with the bat virus RaTG13. They found that although the two were similar in structure, the new coronavirus had a more stable form of glycoprotein, which is about 1,000 times more affinity with the human-like protein ACE2.
    team also found that the Flynn protease cut-off point on the new coronavirus sting may be beneficial to the virus because it may promote the virus's binding to the receptors on the cell. Based on these observations, the researchers believe that bat viruses similar to RaTG13 are less likely to infect human cells.
    So far, scientists don't know how the new coronavirus evolved to infect humans, and it is speculated that there are two mechanisms: to choose between animal hosts (possibly through intermediate hosts) before becoming co-infected with humans, or to make natural choices in humans after being transmitted directly as a co-disease between humans and animals.
    addition, the researchers point out that their new coronavirus pyrethroids have a high resolution, are nearly complete, and have more external rings than previously reported structures, which may be important for current vaccine design.
    This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only. This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed description of the concern or complaint, to service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content will be removed immediately.

    Contact Us

    The source of this page with content of products and services is from Internet, which doesn't represent ECHEMI's opinion. If you have any queries, please write to service@echemi.com. It will be replied within 5 days.

    Moreover, if you find any instances of plagiarism from the page, please send email to service@echemi.com with relevant evidence.