Elastase-mediated activation of the severe acute respiratory syndrome coronavirus spike protein at discrete sites within the S2 domain.
Identifieur interne : 002547 ( Main/Exploration ); précédent : 002546; suivant : 002548Elastase-mediated activation of the severe acute respiratory syndrome coronavirus spike protein at discrete sites within the S2 domain.
Auteurs : Sandrine Belouzard [États-Unis] ; Ikenna Madu ; Gary R. WhittakerSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Bovins, Cellules Vero, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Mutagenèse, Mutation, Pancreatic elastase (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Trypsine (métabolisme), Virus du SRAS (métabolisme), Virus du SRAS (physiologie).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- métabolisme : Glycoprotéines membranaires, Pancreatic elastase, Protéines de l'enveloppe virale, Trypsine, Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Bovins, Cellules Vero, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Mutagenèse, Mutation, Protéines de l'enveloppe virale, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Cattle, Cell Fusion, Chlorocebus aethiops, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mutagenesis, Mutation, Pancreatic Elastase (metabolism), Protein Structure, Tertiary, SARS Virus (metabolism), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Trypsin (metabolism), Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Pancreatic Elastase, Trypsin, Viral Envelope Proteins.
- metabolism : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Binding Sites, Cattle, Cell Fusion, Chlorocebus aethiops, Humans, Mutagenesis, Mutation, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
Proteolytic priming is a common method of controlling the activation of membrane fusion mediated by viral glycoproteins. The severe acute respiratory syndrome coronavirus spike protein (SARS-CoV S) can be primed by a variety of host cell proteases, with proteolytic cleavage occurring both as the S1/S2 boundary and adjacent to a fusion peptide in the S2 domain. Here, we studied the priming of SARS-CoV S by elastase and show an important role for residue Thr(795) in the S2 domain. A series of alanine mutants were generated in the vicinity of the S2 cleavage site, with the goal of examining elastase-mediated cleavage within S2. Both proteolytic cleavage and fusion activation were modulated by altering the cleavage site position. We propose a novel mechanism whereby SARS-CoV fusion protein function can be controlled by spatial regulation of the proteolytic priming site, with important implications for viral pathogenesis.
DOI: 10.1074/jbc.M110.103275
PubMed: 20507992
Affiliations:
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Le document en format XML
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<term>Binding Sites</term>
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<term>Cell Fusion</term>
<term>Chlorocebus aethiops</term>
<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Mutagenesis</term>
<term>Mutation</term>
<term>Pancreatic Elastase (metabolism)</term>
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<term>Viral Envelope Proteins (metabolism)</term>
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<term>Bovins</term>
<term>Cellules Vero</term>
<term>Fusion cellulaire</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
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<term>Virus du SRAS (physiologie)</term>
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<term>Chlorocebus aethiops</term>
<term>Humans</term>
<term>Mutagenesis</term>
<term>Mutation</term>
<term>Protein Structure, Tertiary</term>
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<front><div type="abstract" xml:lang="en">Proteolytic priming is a common method of controlling the activation of membrane fusion mediated by viral glycoproteins. The severe acute respiratory syndrome coronavirus spike protein (SARS-CoV S) can be primed by a variety of host cell proteases, with proteolytic cleavage occurring both as the S1/S2 boundary and adjacent to a fusion peptide in the S2 domain. Here, we studied the priming of SARS-CoV S by elastase and show an important role for residue Thr(795) in the S2 domain. A series of alanine mutants were generated in the vicinity of the S2 cleavage site, with the goal of examining elastase-mediated cleavage within S2. Both proteolytic cleavage and fusion activation were modulated by altering the cleavage site position. We propose a novel mechanism whereby SARS-CoV fusion protein function can be controlled by spatial regulation of the proteolytic priming site, with important implications for viral pathogenesis.</div>
</front>
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