About: Proteolytic Processing of Filovirus Glycoproteins

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About: Proteolytic Processing of Filovirus Glycoproteins 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
has title	Proteolytic Processing of Filovirus Glycoproteins
Creator	Volchkov, Viktor Klenk, Hans Klenk, H Volchkov, V
Source	PMC
abstract	Filoviruses (Marburg virus and Ebola virus) have a single envelope glycoprotein (GP) that initiates infection. GP is a class I fusion protein that forms trimeric spikes composed of heterodimers of the subunits GP1 and GP2. GP1 and GP2 are derived from the precursor pre-GP by furin cleavage during exocytosis. GP1 contains a receptor-binding core topped by a glycan cap and a heavily glycosylated mucin-like domain, while GP2 contains a fusion loop and a membrane anchor. After entering cells by macropinocytosis, the glycan cap and the mucin-like domain are removed from GP1 by endosomal cathepsins B and L exposing the binding site for the Niemann-Pick C1 receptor. It appears that there is no strict requirement for specific proteases involved in GP processing. Thus, furin is not indispensible for GP1-2 cleavage, and GP1 may be trimmed not only by cathepsins B and L but also by other endosomal proteases. Two soluble glycoproteins of Ebola virus are also processed by host proteases. A significant amount of GP1,2 is cleaved by the metalloprotease TACE and shed from the surface of infected cells (GP1,2 delta). The secreted protein sGP is derived from the precursor pre-sGP by furin cleavage.
has issue date	2018-02-16(xsd:dateTime)
bibo:doi	10.1007/978-3-319-75474-1_5
has license	no-cc
sha1sum (hex)	df98ad8bef96d4cef9824d1dc28f47c483e7d5e1
schema:url	https://doi.org/10.1007/978-3-319-75474-1_5
resource representing a document's title	Proteolytic Processing of Filovirus Glycoproteins
has PubMed Central identifier	PMC7122482
schema:publication	Activation of Viruses by Host Proteases
resource representing a document's body	covid:df98ad8bef96d4cef9824d1dc28f47c483e7d5e1#body_text
is schema:about of	named entity 'processing' named entity 'infection' named entity 'Proteolytic' named entity 'EXOCYTOSIS' named entity 'IS A' named entity 'RECEPTOR' named entity 'BINDING SITE' named entity 'CLASS I' named entity 'CATHEPSINS B' named entity 'EBOLA VIRUS' named entity 'cap' named entity 'GP2' named entity 'specific' named entity 'cap' named entity 'cleavage' named entity 'composed' named entity 'After' named entity 'fusion' named entity 'fusion protein' named entity 'Glycoproteins' named entity 'endosomal' named entity 'class I fusion protein' named entity 'Niemann-Pick' named entity 'cleavage' named entity 'Marburg virus' named entity 'glycan' named entity 'trimeric' named entity 'virus' named entity 'transcriptional' named entity 'protein' named entity 'filoviruses' named entity 'thermolysin' named entity 'proteases' named entity 'glycoprotein' named entity 'recombinant' named entity 'small angle X-ray scattering' named entity 'glycan' named entity 'EBOV' named entity 'EBOV' named entity 'furin' named entity 'EBOV' named entity 'cathepsin' named entity 'disulfide bridge' named entity 'virus' named entity 'cell surface' named entity 'furin' named entity 'chalice' named entity 'Volchkova' named entity 'class I fusion protein' named entity 'cysteine' named entity 'virus' named entity 'furin' named entity 'sGP' named entity 'amino acid' named entity 'fission' named entity 'proprotein convertase' named entity 'protease inhibitors' named entity 'amino acids' named entity 'knockout mice' named entity 'furin' named entity 'filovirus' named entity 'endosomal' named entity 'virus replication' named entity 'dendritic cells' named entity 'EBOV' named entity 'endosomes' named entity 'Late endosome' named entity 'GPer' named entity 'macrophages' named entity 'Filoviruses' named entity 'NPC1' named entity 'GP2' named entity 'EBOV' named entity 'polyacrylamide gels' named entity 'Arg' named entity 'EBOV' named entity 'mucin' named entity 'viral entry' named entity 'disulfide bond' named entity 'glycoproteins'

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