About: Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion

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About: Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion
Creator	Du, Lanying Jiang, Shibo Wang, Chao Lu, Lu Xia, Shuai Lan, Qiaoshuai Liu, Meiqin Liu, Shuwen Shi, Zhengli Xu, Wei Zhu, Yun Qin, Chuan Bao, Linlin Qi, Feifei Sun, Fei Feng, Siliang
source	Medline; PMC
abstract	The recent outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 infection in Wuhan, China has posed a serious threat to global public health. To develop specific anti-coronavirus therapeutics and prophylactics, the molecular mechanism that underlies viral infection must first be defined. Therefore, we herein established a SARS-CoV-2 spike (S) protein-mediated cell–cell fusion assay and found that SARS-CoV-2 showed a superior plasma membrane fusion capacity compared to that of SARS-CoV. We solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain. We previously developed a pan-coronavirus fusion inhibitor, EK1, which targeted the HR1 domain and could inhibit infection by divergent human coronaviruses tested, including SARS-CoV and MERS-CoV. Here we generated a series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection with IC50s of 1.3 and 15.8 nM, about 241- and 149-fold more potent than the original EK1 peptide, respectively. EK1C4 was also highly effective against membrane fusion and infection of other human coronavirus pseudoviruses tested, including SARS-CoV and MERS-CoV, as well as SARSr-CoVs, and potently inhibited the replication of 5 live human coronaviruses examined, including SARS-CoV-2. Intranasal application of EK1C4 before or after challenge with HCoV-OC43 protected mice from infection, suggesting that EK1C4 could be used for prevention and treatment of infection by the currently circulating SARS-CoV-2 and other emerging SARSr-CoVs.
has issue date	2020-03-30(xsd:dateTime)
bibo:doi	10.1038/s41422-020-0305-x
bibo:pmid	32231345
has license	cc-by
sha1sum (hex)	4e3112583171740ffa5b9af84fe91e2c648b940f
schema:url	https://doi.org/10.1038/s41422-020-0305-x
resource representing a document's title	Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion
has PubMed Central identifier	PMC7104723
has PubMed identifier	32231345
schema:publication	Cell Res
resource representing a document's body	covid:4e3112583171740ffa5b9af84fe91e2c648b940f#body_text
is schema:about of	named entity 'HR1' named entity 'coronavirus' named entity 'highly' named entity 'infection' named entity 'infection' named entity 'plasma membrane' named entity 'posed' named entity 'tested' named entity 'prevention' named entity 'bundle' named entity 'fusion' named entity 'X-ray' named entity 'fusion inhibitor' named entity 'divergent' named entity 'mice' named entity 'domains' named entity 'interactions' named entity 'HR1' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'emerging' named entity 'highly' named entity 'SARS-CoV-2' named entity 'HR1' named entity 'protein' named entity 'viral infection' named entity 'infection' named entity 'SARS-CoV-2' named entity 'public health' named entity 'HCoV-OC43' named entity 'coronavirus' named entity 'IC50s' named entity 'SARS-CoV-2' named entity 'coronavirus' named entity 'human coronavirus' named entity 'SARS-CoV-2' named entity 'infection' named entity 'spike (S) protein' named entity 'SARS-CoV-2' named entity 'HR1' named entity 'Wuhan' named entity 'helical' named entity 'membrane fusion' named entity 'spike protein' named entity 'coronavirus' named entity 'SARS-CoV-2' named entity 'lipopeptides' named entity 'SARS-CoV-2' named entity 'assay' named entity 'MERS-CoV' named entity 'HR2' named entity 'X-ray crystal structure' named entity 'pseudoviruses' named entity 'protein' named entity 'pseudovirus' named entity 'human coronaviruses' named entity 'SARS-CoV' named entity 'human coronaviruses' named entity 'infection' named entity 'mice' named entity 'fusion inhibitor' named entity 'infection' named entity 'molecular mechanism' named entity 'Intranasal' named entity 'potent' named entity 'MERS-CoV'

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