About: Inhibitors of signal peptide peptidase and subtilisin/kexin-isozyme 1 inhibit Ebola virus glycoprotein-driven cell entry by interfering with activity and cellular localization of endosomal cathepsins

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About: Inhibitors of signal peptide peptidase and subtilisin/kexin-isozyme 1 inhibit Ebola virus glycoprotein-driven cell entry by interfering with activity and cellular localization of endosomal cathepsins 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	Inhibitors of signal peptide peptidase and subtilisin/kexin-isozyme 1 inhibit Ebola virus glycoprotein-driven cell entry by interfering with activity and cellular localization of endosomal cathepsins
Creator	Winkler, Michael Plegge, Teresa Nehlmeier, Inga Gonzá Lez Herná Ndez, Mariana Krü Ger, Pö Hlmann Id, Stefan Spiegel,
Source	Medline; PMC
abstract	Emerging viruses such as severe fever and thrombocytopenia syndrome virus (SFTSV) and Ebola virus (EBOV) are responsible for significant morbidity and mortality. Host cell proteases that process the glycoproteins of these viruses are potential targets for antiviral intervention. The aspartyl protease signal peptide peptidase (SPP) has recently been shown to be required for processing of the glycoprotein precursor, Gn/Gc, of Bunyamwera virus and for viral infectivity. Here, we investigated whether SPP is also required for infectivity of particles bearing SFTSV-Gn/Gc. Entry driven by the EBOV glycoprotein (GP) and the Lassa virus glycoprotein (LASV-GPC) depends on the cysteine proteases cathepsin B and L (CatB/CatL) and the serine protease subtilisin/kexin-isozyme 1 (SKI-1), respectively, and was examined in parallel for control purposes. We found that inhibition of SPP and SKI-1 did not interfere with SFTSV Gn + Gc-driven entry but, unexpectedly, blocked entry mediated by EBOV-GP. The inhibition occurred at the stage of proteolytic activation and the SPP inhibitor was found to block CatL/CatB activity. In contrast, the SKI-1 inhibitor did not interfere with CatB/CatL activity but disrupted CatB localization in endo/lysosomes, the site of EBOV-GP processing. These results underline the potential of protease inhibitors for antiviral therapy but also show that previously characterized compounds might exert broader specificity than initially appreciated and might block viral entry via diverse mechanisms.
has issue date	2019-04-11(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0214968
bibo:pmid	30973897
has license	cc-by
sha1sum (hex)	57739f7172bb6dd11a63147d6bd37a3c227c7bc2
schema:url	https://doi.org/10.1371/journal.pone.0214968
resource representing a document's title	Inhibitors of signal peptide peptidase and subtilisin/kexin-isozyme 1 inhibit Ebola virus glycoprotein-driven cell entry by interfering with activity and cellular localization of endosomal cathepsins
has PubMed Central identifier	PMC6459477
has PubMed identifier	30973897
schema:publication	PLoS One
resource representing a document's body	covid:57739f7172bb6dd11a63147d6bd37a3c227c7bc2#body_text
is schema:about of	named entity 'signal peptide peptidase' named entity 'viruses' named entity 'activity' named entity 'investigated' named entity 'inhibitor' named entity 'mortality' named entity 'mediated' covid:arg/57739f7172bb6dd11a63147d6bd37a3c227c7bc2 named entity 'Ebola virus' named entity 'Oil Plan' named entity 'Germany' named entity 'EBOV' named entity 'lysosomal' named entity 'cysteine protease inhibitor' named entity 'serum' named entity 'plasmid' named entity 'Lamp-1' named entity 'SARS' named entity 'CatL' named entity 'MERS-CoV' named entity 'CatL' named entity 'CatL' named entity 'DMEM' named entity 'experimental settings' named entity '1:400' named entity 'culture medium' named entity 'lysosomal' named entity 'luciferase' named entity 'CatL' named entity 'streptomycin' named entity 'single cells' named entity 'Student's t-test' named entity 'DMSO' named entity 'Democratic Republic of Congo' named entity 'high levels' named entity 'MERS' named entity 'Homo sapiens' named entity 'proteases' named entity 'LASV' named entity 'CatL' named entity 'CatL' named entity 'beetle' named entity 'AMC' named entity 'colocalization' named entity 'CatL' named entity 'infectivity' named entity 'GNPTAB' named entity 'control' named entity 'depends' named entity 'antiviral therapy' named entity 'glycoprotein' named entity 'González' named entity 'potential' named entity 'viral' named entity 'SKI' named entity 'Lassa virus' named entity 'lysosomes' named entity 'luciferase' named entity 'colocalization' named entity 'EBOV' named entity 'cysteine' named entity 'VSV-G' named entity 'standard deviation' named entity 'EBOV' named entity 'host cell' named entity 'CatL' named entity 'EBOV' named entity 'human population' named entity 'Sigma Aldrich' named entity 'Abcam' named entity 'infectivity' named entity 'Cuevavirus' named entity 'fluorophore' named entity 'DMSO' named entity 'EBOV'

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