About: Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit()

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit() Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit()
Creator	Zeng, Fanya Chan, Chi, Frederick Hon, Chung Kwok, Hung Leung, Ching Peiris, Joseph Yip, Chi Law, Ka Yeung, Shan
Source	Elsevier; Medline; PMC
abstract	Neutralizing effects of antibodies targeting the C-terminal stalk (S2) subunit of the spike protein of severe acute respiratory syndrome coronavirus have previously been reported, although its mechanism remained elusive. In this study, high titered mouse antisera against the N-terminal globular (S1) and S2 subunits of the S protein were generated and total immunoglobulin G (IgG) was purified from these antisera. The efficiency of these purified IgGs in virus neutralization and blocking of receptor binding were compared quantitatively using virus neutralization assay and a previously developed cell-based receptor binding assay, respectively. We demonstrated that anti-S1 IgG neutralizes the virus and binds to the membrane associated S protein more efficiently than anti-S2 IgG does. Moreover, both anti-S1 and anti-S2 IgGs were able to abolish the binding between S protein and its cellular receptor(s), although anti-S1 IgG showed a significantly higher blocking efficiency. The unexpected blocking ability of anti-S2 IgG towards the receptor binding implied a possible role of the S2 subunit in virus docking process and argues against the current hypothesis of viral entry. On the other hand, the functional roles of the previously reported neutralizing epitopes within S2 subunit were investigated using an antigen specific antibody depletion assay. Depletion of antibodies against these regions significantly diminished, though not completely abolished, the neutralizing effects of anti-S2 IgG. It suggests the absence of a major neutralizing domain on S2 protein. The possible ways of anti-S2 IgGs to abolish the receptor binding and the factors restricting anti-S2 IgGs to neutralize the virus are discussed.
has issue date	2006-10-16(xsd:dateTime)
bibo:doi	10.1016/j.febslet.2006.08.085
bibo:pmid	16989815
has license	no-cc
sha1sum (hex)	9115f3c9be874d41c7f9f31bc7e54ab2a92d6aa6
schema:url	https://doi.org/10.1016/j.febslet.2006.08.085
resource representing a document's title	Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit()
has PubMed Central identifier	PMC7094555
has PubMed identifier	16989815
schema:publication	FEBS Lett
resource representing a document's body	covid:9115f3c9be874d41c7f9f31bc7e54ab2a92d6aa6#body_text
is schema:about of	named entity 'neutralization' named entity 'mouse' named entity 'developed' named entity 'neutralization' named entity 'DOCKING' named entity 'elusive' named entity 'efficiency' named entity 'implied' named entity 'functional' named entity 'subunit' named entity 'targeting' named entity 'subunit' named entity 'virus' named entity 'cell-based' named entity 'protein' named entity 'N-terminal' named entity 'protein' named entity 'assay' named entity 'receptor binding' named entity 'receptor binding assay' named entity 'antisera' named entity 'protein' named entity 'cellular receptor' named entity 'IgG' named entity 'antibodies' named entity 'spike protein' named entity 'agarose' named entity 'coronavirus' named entity 'flow cytometer' named entity 'FITC' named entity 'antibodies' named entity 'SARS-CoV' named entity 'antibodies' named entity 'antisera' named entity 'antibodies' named entity 'antibodies' named entity 'significant difference' named entity 'amino acids' named entity 'membrane fusion' named entity 'IgG' named entity 'nucleocapsid' named entity 'SARS-CoV' named entity 'cell-cell' named entity 'antisera' named entity 'His-tag' named entity 'transduced' named entity 'antigens' named entity 'epitopes' named entity 'rational design' named entity 'protein' named entity 'native structure' named entity 'emerging infectious disease' named entity 'protein' named entity 'antibodies' named entity 'NIH' named entity 'transduced' named entity 'oligosaccharides' named entity 'virus' named entity 'FACS' named entity 'SARS-CoV' named entity 'Escherichia coli' named entity 'protein' named entity 'protein' named entity 'IgG' named entity 'cell-based' named entity 'IgG' named entity 'control group' named entity 'peptide' named entity 'BALB/c' named entity 'mice' named entity 'ATCC' named entity 'ATCC'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software