Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.
Identifieur interne : 001480 ( PubMed/Corpus ); précédent : 001479; suivant : 001481Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.
Auteurs : Kazuya Shirato ; Madoka Maejima ; Shutoku Matsuyama ; Makoto Ujike ; Ayako Miyazaki ; Natsumi Takeyama ; Hidetoshi Ikeda ; Fumihiro TaguchiSource :
- Virus research [ 1872-7492 ] ; 2011.
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
Links to Exploration step
pubmed:21840351Le document en format XML
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last="Ujike">Makoto Ujike</name></author><author><name sortKey="Miyazaki, Ayako" sort="Miyazaki, Ayako" uniqKey="Miyazaki A" first="Ayako" last="Miyazaki">Ayako Miyazaki</name></author><author><name sortKey="Takeyama, Natsumi" sort="Takeyama, Natsumi" uniqKey="Takeyama N" first="Natsumi" last="Takeyama">Natsumi Takeyama</name></author><author><name sortKey="Ikeda, Hidetoshi" sort="Ikeda, Hidetoshi" uniqKey="Ikeda H" first="Hidetoshi" last="Ikeda">Hidetoshi Ikeda</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21840351</idno><idno type="pmid">21840351</idno><idno type="doi">10.1016/j.virusres.2011.07.019</idno><idno type="wicri:Area/PubMed/Corpus">001480</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" 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Makoto" uniqKey="Ujike M" first="Makoto" last="Ujike">Makoto Ujike</name></author><author><name sortKey="Miyazaki, Ayako" sort="Miyazaki, Ayako" uniqKey="Miyazaki A" first="Ayako" last="Miyazaki">Ayako Miyazaki</name></author><author><name sortKey="Takeyama, Natsumi" sort="Takeyama, Natsumi" uniqKey="Takeyama N" first="Natsumi" last="Takeyama">Natsumi Takeyama</name></author><author><name sortKey="Ikeda, Hidetoshi" sort="Ikeda, Hidetoshi" uniqKey="Ikeda H" first="Hidetoshi" last="Ikeda">Hidetoshi Ikeda</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author></analytic><series><title level="j">Virus research</title><idno type="eISSN">1872-7492</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Coronavirus Infections (veterinary)</term><term>Coronavirus Infections (virology)</term><term>Cytoplasm (virology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Sequence Data</term><term>Mutation, Missense</term><term>Porcine epidemic diarrhea virus (genetics)</term><term>Porcine epidemic diarrhea virus (physiology)</term><term>Protein Sorting Signals</term><term>Protein Transport</term><term>Spike Glycoprotein, Coronavirus</term><term>Swine</term><term>Swine Diseases (virology)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Porcine epidemic diarrhea virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Porcine epidemic diarrhea virus</term></keywords><keywords scheme="MESH" qualifier="veterinary" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term><term>Cytoplasm</term><term>Swine Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Molecular Sequence Data</term><term>Mutation, Missense</term><term>Protein Sorting Signals</term><term>Protein Transport</term><term>Spike Glycoprotein, Coronavirus</term><term>Swine</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21840351</PMID><DateCompleted><Year>2012</Year><Month>01</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7492</ISSN><JournalIssue CitedMedium="Internet"><Volume>161</Volume><Issue>2</Issue><PubDate><Year>2011</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.</ArticleTitle><Pagination><MedlinePgn>188-93</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2011.07.019</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shirato</LastName><ForeName>Kazuya</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama, Tokyo 208-0011, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maejima</LastName><ForeName>Madoka</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Matsuyama</LastName><ForeName>Shutoku</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ujike</LastName><ForeName>Makoto</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Miyazaki</LastName><ForeName>Ayako</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Takeyama</LastName><ForeName>Natsumi</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ikeda</LastName><ForeName>Hidetoshi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Taguchi</LastName><ForeName>Fumihiro</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>08</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane 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