echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Active Ingredient News > Immunology News > Cell: Structurally reveals the human antibody characteristics of the SARS-CoV-2 stingprotein.

    Cell: Structurally reveals the human antibody characteristics of the SARS-CoV-2 stingprotein.

    • Last Update: 2020-07-19
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com

    , June 25, 2020 /
    Biovalley
    BIOON/--- Since December 8, 2019, several cases of pneumonia with unknown etiology have been reported in Wuhan, Hubei Province, ChinaMost of the patients work edtherece at or near the local South China Seafood Wholesale MarketIn the early stages of this pneumonia, severe symptoms of acute respiratory infections develop, and some patients develop rapidly into acute respiratory distress syndrome, ARDS, acute respiratory failure and other serious complicationsOn January 7, 2020, the China Center for Disease Control and Prevention (CDC) identified a new coronavirus from a patient's pharynx sample, initially named 2019-nCoV by the World Health Organization (WHO)Most patients with 2019-nCoV pneumonia have mild symptoms and a good prognosisSo far, some patients have developed severe pneumonia, pulmonary edema, ARDS or multiple organ failure and death11 February 2020, WHO renamed the disease 2019 coronavirus disease (COVID-19)On the same day, the Coronary Virus Research Group of the International Committee on Virus Classification and Naming viruses published an article in bioRxiv, noting that the team had decided that the new coronavirus 2019-nCoV was a variant of the 2002-2003 outbreak of severe acute respiratory syndrome (SARS)-CoVTherefore, the new pathogen was renamed Severe Acute Respiratory Syndrome Coronavirus 2, or SARS-CoV-2picture source: fr.wikipedia.orgcoronavirus can cause multi-system infections in a variety of animalsPrior to this, there were six coronaviruses that could infect humans, mainly causing respiratory infections in humans: two highly deadly coronaviruses, severe acute respiratory syndrome (SARS-CoV) and MERS (MERS) coronaviruses (MERS-CoV);coronavirus enters the host cell is mediated by the virus's sting protein (S protein), which forms a tripolymer sting on the surface of the virusEach monomer in the triple-poly S protein assembly is a heterogenous dipolymer consisting of S1 and S2 subkeysThe S1 subkey consists of four domains: the N-end domain (NTD), the C-side domain (CTD), and the sub-domainiareas I and II Both SARS-CoV and SARS-CoV-2 CTD function as receptor binding domain (RBD) and are used to bind the same entry receptor --- human angiotensin transeronose 2 (hACE2) S2 subkeys contain fusion peptides, octapeptide repeat zones 1 and 2, and a trans-membrane domain, all of which are required for the fusion of viral and host cell membranes The neutralizing antibody response to coronaviruses mainly targets THE RBD of the tripolymer S protein in a new study , researchers from the California Institute of Technology and Rockefeller University described the identification of polyclonal IgG and their Fab fragments from the plasma of COVID-19 recoverers for the coronavirus S protein They found that these plasma IgGs identify edited S proteins for SARS-CoV-2, SARS-CoV, and MERS-CoV related findings published online June 23, 2020 in the journal Cell, with the title "Structures of Human antibodies to SARS-CoV-Spike 2 Reveal Common sphotos and recurrent sons of antibodies" The paper's authors are Dr Michel C Nussenzweig of Rockefeller University and Dr Pamela J Bjorkman of the California Institute of Technology The paper's first author is Christopher O Barnes of the California Institute of Technology differ in the contribution of plasma IgG to targeting RBD epitopes, identifying alpha and beta coronaviruses, and affinity to binding/neutralization enhancement compared to Fab fragments using electron microscopes, the researchers studied the specificity of the plasma polyclonal antibody Fab fragments, revealing that they identify s1A and RBD epitopes on the surface of the SARS-CoV-2 S protein In addition, the cryoscopy (cryo-EM) structure of the single-clone neutralized and antibody Fab fragment-prion protein complex with a resolution of 3.4 e revealed a epitope that blocks the binding of ACE2 receptors Modeling based on these structures shows that IgG has different potential for S-protein crosslinking on the surface of the coronavirus than fab fragments, and that IgG may not be affected by the identified SARS-CoV-2 S protein mutation overall, the study structurally identified a recurring anti-SARS-CoV-2 antibody category derived from VH3-53/VH3-66, and its similarity to SARS-CoV VH3-30 antibodies, which provides a standard for evaluating vaccine-induced antibodies (Biological Valley Bioon.com) References: Christopher O Barnes et , Structures of human anti-bounds to SARS-CoV-2 spike-reveal common epitopes and rephotos of the antibodies Cell, 2020, doi: 10.1016/j.cell.2020.06.025.
    .
    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.