Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.
Identifieur interne : 002077 ( Main/Exploration ); précédent : 002076; suivant : 002078Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.
Auteurs : Kazuya Shirato [Japon] ; Madoka Maejima ; Shutoku Matsuyama ; Makoto Ujike ; Ayako Miyazaki ; Natsumi Takeyama ; Hidetoshi Ikeda ; Fumihiro TaguchiSource :
- Virus research [ 1872-7492 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Cytoplasme (virologie), Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Infections à coronavirus (médecine vétérinaire), Infections à coronavirus (virologie), Lignée cellulaire, Maladies des porcs (virologie), Mutation faux-sens, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Pénétration virale, Signaux de triage des protéines, Suidae, Séquence d'acides aminés, Transport de protéines, Virus de la diarrhée porcine épidémique (génétique), Virus de la diarrhée porcine épidémique (physiologie).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de la diarrhée porcine épidémique.
- médecine vétérinaire : Infections à coronavirus.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- physiologie : Virus de la diarrhée porcine épidémique.
- virologie : Cytoplasme, Infections à coronavirus, Maladies des porcs.
- Animaux, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Lignée cellulaire, Mutation faux-sens, Protéines de l'enveloppe virale, Pénétration virale, Signaux de triage des protéines, Suidae, Séquence d'acides aminés, Transport de protéines.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Coronavirus Infections (veterinary), Coronavirus Infections (virology), Cytoplasm (virology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Mutation, Missense, Porcine epidemic diarrhea virus (genetics), Porcine epidemic diarrhea virus (physiology), Protein Sorting Signals, Protein Transport, Spike Glycoprotein, Coronavirus, Swine, Swine Diseases (virology), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : Porcine epidemic diarrhea virus.
- physiology : Porcine epidemic diarrhea virus.
- veterinary : Coronavirus Infections.
- virology : Coronavirus Infections, Cytoplasm, Swine Diseases.
- Amino Acid Sequence, Animals, Cell Line, Molecular Sequence Data, Mutation, Missense, Protein Sorting Signals, Protein Transport, Spike Glycoprotein, Coronavirus, Swine, Virus Internalization.
Abstract
Murine-adapted porcine epidemic diarrhea virus (PEDV), MK-p10, shows high neurovirulence and increased fusion activity compared with a non-adapted MK strain. MK-p10 S protein had four mutations relative to the original virus S, and one of these (H→R at position 1381, H1381R) in the cytoplasmic tail (CT) was suggested to be responsible for the increased fusion activity. To explore this, we examined fusion activity using recombinant S proteins. We expressed and compared the fusion activity of MK-p10 S, S with the H1381R mutation, S with the three other mutations that were not thought to be involved in high fusion activity, and the original S protein. The MK-p10 and MK-H1381R S proteins induced larger cell fusions than others. We also examined the distribution of these S proteins; the MK-p10 and MK-H1381R S proteins were transported onto the cell surface more efficiently than others. These findings suggest that the H1381R mutation is responsible for enhanced fusion activity, which may be attributed to the efficient transfer of S onto the cell surface. H1381 is a component of the KxHxx motif in the CT region, which is a retrieval signal of the S protein for the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). Loss of this motif could allow for the efficient transfer of S proteins from ERGIC onto the cell surface and subsequent increased fusion activity.
DOI: 10.1016/j.virusres.2011.07.019
PubMed: 21840351
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Murine-adapted porcine epidemic diarrhea virus (PEDV), MK-p10, shows high neurovirulence and increased fusion activity compared with a non-adapted MK strain. MK-p10 S protein had four mutations relative to the original virus S, and one of these (H→R at position 1381, H1381R) in the cytoplasmic tail (CT) was suggested to be responsible for the increased fusion activity. To explore this, we examined fusion activity using recombinant S proteins. We expressed and compared the fusion activity of MK-p10 S, S with the H1381R mutation, S with the three other mutations that were not thought to be involved in high fusion activity, and the original S protein. The MK-p10 and MK-H1381R S proteins induced larger cell fusions than others. We also examined the distribution of these S proteins; the MK-p10 and MK-H1381R S proteins were transported onto the cell surface more efficiently than others. These findings suggest that the H1381R mutation is responsible for enhanced fusion activity, which may be attributed to the efficient transfer of S onto the cell surface. H1381 is a component of the KxHxx motif in the CT region, which is a retrieval signal of the S protein for the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). Loss of this motif could allow for the efficient transfer of S proteins from ERGIC onto the cell surface and subsequent increased fusion activity.</div>
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<name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name>
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<name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name>
<name sortKey="Takeyama, Natsumi" sort="Takeyama, Natsumi" uniqKey="Takeyama N" first="Natsumi" last="Takeyama">Natsumi Takeyama</name>
<name sortKey="Ujike, Makoto" sort="Ujike, Makoto" uniqKey="Ujike M" first="Makoto" last="Ujike">Makoto Ujike</name>
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<country name="Japon"><region name="Région de Kantō"><name sortKey="Shirato, Kazuya" sort="Shirato, Kazuya" uniqKey="Shirato K" first="Kazuya" last="Shirato">Kazuya Shirato</name>
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