About: Structural Molecular Insights into SARS Coronavirus Cellular Attachment, Entry and Morphogenesis

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

About: Structural Molecular Insights into SARS Coronavirus Cellular Attachment, Entry and Morphogenesis 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
title	Structural Molecular Insights into SARS Coronavirus Cellular Attachment, Entry and Morphogenesis
Creator	Beniac, Daniel Booth, T Booth, Timothy Lal, S
source	PMC
abstract	Coronavirus spikes have the largest mass of any known viral spike molecule. The spike is a type 1 viral fusion protein, a class of trimeric surface glycoprotein proteins from diverse viral families that share many common structural and functional characteristics. Fusion proteins are mainly responsible for host cell receptor recognition and subsequent membrane fusion, and may perform other roles such as virus assembly and release via budding. The conformational changes that occur in the spike of intact SARS coronavirus (SARS-CoV) when it binds to the viral receptor, angiotensin-converting enzyme 2 (ACE2) are described. Clues to the structural/functional relationships of membrane fusion have been made possible by the development of viral purification and inactivation methods, along with cryo-electron microscopy (cryo-EM) and three-dimensional (3D) image processing of many different images containing multiple views of the spikes. These methods have allowed study of the spikes while still attached to virions that are noninfectious, but fusionally competent. The receptor-binding and fusion core domains within the SARS-CoV spike have been precisely localized within the spike. Receptor binding results in structural changes that have been observed in the spike molecule, and these appear to be the initial step in viral membrane fusion. A working model for the stepwise process of receptor binding, and subsequent membrane fusion in SARS-CoV is presented. Uniquely, the large size of the SARS-CoV spike allows structural changes to be observed by cryo-EM in the native state. This provides a useful model for studying the basic process of membrane fusion in general, which forms an essential part of the function of many cellular processes.
has issue date	2009-07-22(xsd:dateTime)
bibo:doi	10.1007/978-3-642-03683-5_3
has license	no-cc
sha1sum (hex)	1e3c2038cb24a74a867fbc8e1c753f97901d0dd5
schema:url	https://doi.org/10.1007/978-3-642-03683-5_3
resource representing a document's title	Structural Molecular Insights into SARS Coronavirus Cellular Attachment, Entry and Morphogenesis
has PubMed Central identifier	PMC7176236
schema:publication	Molecular Biology of the SARS-Coronavirus
resource representing a document's body	covid:1e3c2038cb24a74a867fbc8e1c753f97901d0dd5#body_text
is schema:about of	named entity 'spikes' named entity 'cryo-EM' named entity 'surface' named entity 'membrane fusion' named entity 'molecule' named entity 'SARS-CoV' named entity 'The' named entity 'receptor' named entity 'mass' named entity 'SARS Coronavirus' named entity 'DESCRIBED' named entity 'RESPONSIBLE' named entity 'SARS-COV' named entity 'ROLES' named entity 'STUDY' named entity 'CORE' named entity 'SPIKES' named entity 'OCCUR' named entity 'PRESENTED' named entity 'CONTAINING' named entity 'VIRAL' named entity 'PROCESS' named entity 'NATIVE' named entity 'STRUCTURAL' covid:arg/1e3c2038cb24a74a867fbc8e1c753f97901d0dd5 named entity 'viral' named entity 'spike' named entity 'viral' named entity 'conformational' named entity 'observed' named entity 'spike' named entity 'domains' named entity 'Mrad' named entity 'image processing' named entity 'fusion peptide' named entity 'SARS-CoV' named entity 'structural proteins' named entity 'axis of symmetry' named entity 'attached' named entity 'cellular processes' named entity 'The' named entity 'image processing' named entity 'release' named entity 'spike' named entity 'spikes' named entity 'SARS coronavirus' named entity 'virus' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'fusion core' named entity 'Coronavirus' named entity 'membrane fusion' named entity 'receptor binding' named entity 'fusion protein' named entity 'glycoprotein' named entity 'native state' named entity 'ACE2' named entity 'Morphogenesis' named entity 'SARS' named entity '3D structures' named entity 'cryo-EM' named entity 'type 1' named entity 'protein' named entity 'host membrane' named entity 'peptide cleavage' named entity 'type 1' named entity 'host membrane' named entity 'cell surface' named entity 'ACE2' named entity 'phylogenetic' named entity 'ACE2' named entity 'blue line' named entity 'virion' named entity 'fusion core' named entity 'cell-surface' named entity 'membrane fusion' named entity 'molecule' named entity 'virions' named entity 'redox conditions' named entity 'HR2'

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