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Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.

Identifieur interne : 001822 ( PubMed/Curation ); précédent : 001821; suivant : 001823

Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.

Auteurs : Jean Kaoru Millet [États-Unis] ; Gary R. Whittaker [États-Unis]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2014.

RBID : pubmed:25288733

Descripteurs français

English descriptors

KwdEn :
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Computational Biology, Furin (chemistry), Gene Silencing, Genetic Predisposition to Disease, HEK293 Cells, Humans, Middle East Respiratory Syndrome Coronavirus (physiology), Mutation, Peptide Hydrolases (metabolism), RNA, Small Interfering (metabolism), Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus (metabolism), Time Factors, Vero Cells, Virus Internalization.
MESH :
- chemical , chemistry : Furin.
- chemical , metabolism : Peptide Hydrolases, RNA, Small Interfering, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Computational Biology, Gene Silencing, Genetic Predisposition to Disease, HEK293 Cells, Humans, Mutation, Time Factors, Vero Cells, Virus Internalization.

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified betacoronavirus causing high morbidity and mortality in humans. The coronavirus spike (S) protein is the main determinant of viral entry, and although it was previously shown that MERS-CoV S can be activated by various proteases, the details of the mechanisms of proteolytic activation of fusion are still incompletely characterized. Here, we have uncovered distinctive characteristics of MERS-CoV S. We identify, by bioinformatics and peptide cleavage assays, two cleavage sites for furin, a ubiquitously expressed protease, which are located at the S1/S2 interface and at the S2' position of the S protein. We show that although the S1/S2 site is proteolytically processed by furin during protein biosynthesis, the S2' site is cleaved upon viral entry. MERS-CoV pseudovirion infection was shown to be enhanced by elevated levels of furin expression, and entry could be decreased by furin siRNA silencing. Enhanced furin activity appeared to partially override the low pH-dependent nature of MERS-CoV entry. Inhibition of furin activity was shown to decrease MERS-CoV S-mediated entry, as well as infection by the virus. Overall, we show that MERS-CoV has evolved an unusual two-step furin activation for fusion, suggestive of a role during the process of emergence into the human population. The ability of MERS-CoV to use furin in this manner, along with other proteases, may explain the polytropic nature of the virus.

DOI: 10.1073/pnas.1407087111
PubMed: 25288733

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<term>Facteurs temps</term>
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<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified betacoronavirus causing high morbidity and mortality in humans. The coronavirus spike (S) protein is the main determinant of viral entry, and although it was previously shown that MERS-CoV S can be activated by various proteases, the details of the mechanisms of proteolytic activation of fusion are still incompletely characterized. Here, we have uncovered distinctive characteristics of MERS-CoV S. We identify, by bioinformatics and peptide cleavage assays, two cleavage sites for furin, a ubiquitously expressed protease, which are located at the S1/S2 interface and at the S2' position of the S protein. We show that although the S1/S2 site is proteolytically processed by furin during protein biosynthesis, the S2' site is cleaved upon viral entry. MERS-CoV pseudovirion infection was shown to be enhanced by elevated levels of furin expression, and entry could be decreased by furin siRNA silencing. Enhanced furin activity appeared to partially override the low pH-dependent nature of MERS-CoV entry. Inhibition of furin activity was shown to decrease MERS-CoV S-mediated entry, as well as infection by the virus. Overall, we show that MERS-CoV has evolved an unusual two-step furin activation for fusion, suggestive of a role during the process of emergence into the human population. The ability of MERS-CoV to use furin in this manner, along with other proteases, may explain the polytropic nature of the virus. </div>
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<Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified betacoronavirus causing high morbidity and mortality in humans. The coronavirus spike (S) protein is the main determinant of viral entry, and although it was previously shown that MERS-CoV S can be activated by various proteases, the details of the mechanisms of proteolytic activation of fusion are still incompletely characterized. Here, we have uncovered distinctive characteristics of MERS-CoV S. We identify, by bioinformatics and peptide cleavage assays, two cleavage sites for furin, a ubiquitously expressed protease, which are located at the S1/S2 interface and at the S2' position of the S protein. We show that although the S1/S2 site is proteolytically processed by furin during protein biosynthesis, the S2' site is cleaved upon viral entry. MERS-CoV pseudovirion infection was shown to be enhanced by elevated levels of furin expression, and entry could be decreased by furin siRNA silencing. Enhanced furin activity appeared to partially override the low pH-dependent nature of MERS-CoV entry. Inhibition of furin activity was shown to decrease MERS-CoV S-mediated entry, as well as infection by the virus. Overall, we show that MERS-CoV has evolved an unusual two-step furin activation for fusion, suggestive of a role during the process of emergence into the human population. The ability of MERS-CoV to use furin in this manner, along with other proteases, may explain the polytropic nature of the virus. </AbstractText>
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HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001822 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 001822 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    PubMed
   |étape=   Curation
   |type=    RBID
   |clé=     pubmed:25288733
   |texte=   Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i   -Sk "pubmed:25288733" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.

Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki