About: D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity

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

About: D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity 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	D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity
Creator	Wang, Kai Chen, Juan Hu, Jie Tang, Deng, Hai-Jun »more»
source	BioRxiv
abstract	Coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The spike (S) protein that mediates SARS-CoV-2 entry into host cells is a major target for vaccines and therapeutics. Thus, insights into its sequence variations are key to understanding the infection and antigenicity of SARS-CoV-2. A dominant mutational variant at position 614 of the S protein (aspartate to glycine, D614G mutation) was observed in the SARS-CoV-2 genome sequence obtained from the Nextstrain database. Using a pseudovirus-based assay, we identified that S-D614 and S-G614 protein pseudotyped viruses share a common receptor, human angiotensin-converting enzyme 2 (ACE2), which could be blocked by recombinant ACE2 with the fused Fc region of human IgG1. However, S-D614 and S-G614 protein demonstrated functional differences. First, S-G614 protein could be cleaved by serine protease elastase-2 more efficiently. Second, S-G614 pseudovirus infected 293T-ACE2 cells significantly more efficiently than did the S-D614 pseudovirus, especially in the presence of elastase-2. Third, an elastase inhibitor approved for clinical use blocked elastase-enhanced S-G614 pseudovirus infection. Moreover, 93% (65/70) convalescent sera from patients with COVID-19 could neutralize both S-D614 and S-G614 pseudoviruses with comparable efficiencies, but about 7% (5/70) convalescent sera showed reduced neutralizing activity against the S-G614 pseudovirus. These findings have important implications for SARS-CoV-2 transmission and immune interventions.
has issue date	2020-07-06(xsd:dateTime)
bibo:doi	10.1101/2020.06.20.161323
has license	biorxiv
sha1sum (hex)	e8339d5bf800131190a288f59bd81418d1c7804d
schema:url	https://doi.org/10.1101/2020.06.20.161323
resource representing a document's title	D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity
schema:publication	bioRxiv
resource representing a document's body	covid:e8339d5bf800131190a288f59bd81418d1c7804d#body_text
is schema:about of	named entity 'pseudoviruses' named entity 'elastase' named entity 'pseudovirus' named entity 'ACE2' named entity 'SARS' »more»

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 © 2009-2025 OpenLink Software