echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Active Ingredient News > Infection > Cell: Uncovering the true face of Lushan, Li Lanxuan/Li Sai analyzed the complete molecular structure of the new coronavirus for the first time.

    Cell: Uncovering the true face of Lushan, Li Lanxuan/Li Sai analyzed the complete molecular structure of the new coronavirus for the first time.

    • Last Update: 2020-10-01
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    The new coronavirus (SARS-CoV-2) is the pathogen that causes the current COVID-19 epidemic, and is a new type of beta coronavirus.
    With the joint efforts of scientists around the world, much progress has been made in clarifying the protein structure of the new coronavirus, and it has been determined that the new coronavirus genome encodes 29 proteins, four of which are structural proteins, namely: hedgehog protein (S protein), nucleoprotein (N protein), membrane protein (M protein) and envelope protein (E protein).
    , however, the full detailed structure of the new coronavirus has yet to be revealed.
    September 14, 2020, Li Lanxuan, a member of Zhejiang University's National Key Laboratory for infectious disease diagnosis and treatment, and Li Sai, a researcher at Tsinghua University's School of Health Sciences, jointly published a research paper entitled: Molecular architecture of SARS-CoV-2 virus in cell magazine, a leading international academic journal.
    the study used cryo-ET and sub-fault scanning graph averaging (STA) to analyze the molecular assembly of real new coronavirus.
    very detailed picture of the complete structure of the new coronavirus, revealing how the new coronavirus accumulated a 30kb long RNA genome in an inner cavity only 80nm in diameter.
    protein of about 600 kDa is one of the largest known Class I fusion proteins, which is highly glycosylated by 66 N-connected polysaccharides.
    S protein invades cells by binding to the cell surface bind domain (RBD) and the cell surface-like ligandion conversion enzyme 2 (ACE2).
    Although researchers have parsed the mechanism of identification and intrusion of the new coronavirus into the host by recombining proteins near atomic resolution, we still need high-resolution in-place structural information for true viruses.
    coronavirus has the largest genome of any RNA virus.
    how its nuclear crust protein (N protein) oligomers in viruses, tissue and package up to 30kb of single-stranded RNA, it is inexplicable.
    so far, there are no molecular models of RNA proteins (RPPs) for coronavirus, and little is known about the RNP structure, assembly, and RNA packaging of other RNA viruses.
    to address these issues, the team combined cryo-ET and sub-fault scanning imaging (STA) to image 2,294 complete virus particles bred from early new coronavirus strains.
    the study identified the natural structure before and after fusion of the new coronavirus prickly protein (S protein) and the host cell ACE2 protein, with an average resolution of 8.7-11.
    analysis of the composition of N-linked polysaccharose from natural stings by mass spectrometrometrometra revealed that the overall processing status of natural polysaccharose and recombined glycosaccharin polysaccharin was highly similar.
    the study also analyzed the natural composition and advanced structure of the nuclear kernel protein (RNP).
    at the 2D level, there are three combinations of CYP (RNP), namely, next to the cytosome protein packaging, hexagon, triangle.
    at the 3D level, RNP near the membrane forms a heteral structure similar to that of an egg in a nest, while membrane-free RNP forms a pyramid-shaped tesome structure.
    most hexaphdes come from spherical viruses, while more tesomes come from spheroidal viruses.
    statistical analysis shows that spheroidal viruses tend to accumulate more RNP tyres.
    In addition, the spacing between the two adjacent RNPs of the tesome and heteosomes is the same, both 18nm, and some tesomes can be assembled into heteosomes, indicating that the RNP tessome is a virus-critical and basic packaging unit.
    the study analyzed the molecular assembly of the real new coronavirus, mapping in great detail the complete structure of the new coronavirus and revealing how the new coronavirus accumulated a 30kb long RNA genome in an inner cavity only 80nm in diameter.
    the study built the largest cryo-ET data set of the new coronavirus to date.
    also provides new models for future complete viral molecular dynamics simulations, 3D printing, and educational or public media.
    .
    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.