JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells.
Identifieur interne : 002716 ( PubMed/Corpus ); précédent : 002715; suivant : 002717JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells.
Auteurs : Tetsuya Mizutani ; Shuetsu Fukushi ; Masayuki Saijo ; Ichiro Kurane ; Shigeru MorikawaSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2005.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, JNK Mitogen-Activated Protein Kinases (metabolism), Phosphatidylinositol 3-Kinases (metabolism), Protein-Serine-Threonine Kinases (metabolism), Proto-Oncogene Proteins (metabolism), Proto-Oncogene Proteins c-akt, SARS Virus (pathogenicity), Signal Transduction, Vero Cells.
- MESH :
- chemical , metabolism : JNK Mitogen-Activated Protein Kinases, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins.
- metabolism : Phosphatidylinositol 3-Kinases.
- pathogenicity : SARS Virus.
- Animals, Chlorocebus aethiops, Proto-Oncogene Proteins c-akt, Signal Transduction, Vero Cells.
Abstract
Persistence was established after most of the SARS-CoV-infected Vero E6 cells died. RNA of the defective interfering virus was not observed in the persistently infected cells by Northern blot analysis. SARS-CoV diluted to 2 PFU failed to establish persistence, suggesting that some particular viruses in the seed virus did not induce persistent infection. Interestingly, a viral receptor, angiotensin converting enzyme (ACE)-2, was down-regulated in persistently infected cells. G418-selected clones established from parent Vero E6 cells, which were transfected with a plasmid containing the neomycin resistance gene, were infected with SARS-CoV, resulting in a potential cell population capable of persistence in Vero E6 cells. Our previous studies demonstrated that signaling pathways of extracellular signal-related kinase (ERK1/2), c-Jun N-terminal protein kinase (JNK), p38 mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3'-kinase (PI3K)/Akt were activated in SARS-CoV-infected Vero E6 cells. Previous studies also showed that the activation of p38 MAPK by viral infection-induced apoptosis, and a weak activation of Akt was not sufficient to protect from apoptosis. In the present study, we showed that the inhibitors of JNK and PI3K/Akt inhibited the establishment of persistence, but those of MAPK/ERK kinase (MEK; as an inhibitor for ERK1/2) and p38 MAPK did not. These results indicated that two signaling pathways of JNK and PI3K/Akt were important for the establishment of persistence in Vero E6 cells.
DOI: 10.1016/j.bbadis.2005.04.004
PubMed: 15916886
Links to Exploration step
pubmed:15916886Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells.</title>
<author><name sortKey="Mizutani, Tetsuya" sort="Mizutani, Tetsuya" uniqKey="Mizutani T" first="Tetsuya" last="Mizutani">Tetsuya Mizutani</name>
<affiliation><nlm:affiliation>Special Pathogens Laboratory, Department of Virology 1, National Institute of Infectious Diseases, Musashimurayama, Tokyo 208-0011, Japan. tmizutan@nih.go.jp</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Fukushi, Shuetsu" sort="Fukushi, Shuetsu" uniqKey="Fukushi S" first="Shuetsu" last="Fukushi">Shuetsu Fukushi</name>
</author>
<author><name sortKey="Saijo, Masayuki" sort="Saijo, Masayuki" uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name>
</author>
<author><name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name>
</author>
<author><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2005">2005</date>
<idno type="RBID">pubmed:15916886</idno>
<idno type="pmid">15916886</idno>
<idno type="doi">10.1016/j.bbadis.2005.04.004</idno>
<idno type="wicri:Area/PubMed/Corpus">002716</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002716</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells.</title>
<author><name sortKey="Mizutani, Tetsuya" sort="Mizutani, Tetsuya" uniqKey="Mizutani T" first="Tetsuya" last="Mizutani">Tetsuya Mizutani</name>
<affiliation><nlm:affiliation>Special Pathogens Laboratory, Department of Virology 1, National Institute of Infectious Diseases, Musashimurayama, Tokyo 208-0011, Japan. tmizutan@nih.go.jp</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Fukushi, Shuetsu" sort="Fukushi, Shuetsu" uniqKey="Fukushi S" first="Shuetsu" last="Fukushi">Shuetsu Fukushi</name>
</author>
<author><name sortKey="Saijo, Masayuki" sort="Saijo, Masayuki" uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name>
</author>
<author><name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name>
</author>
<author><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name>
</author>
</analytic>
<series><title level="j">Biochimica et biophysica acta</title>
<idno type="ISSN">0006-3002</idno>
<imprint><date when="2005" type="published">2005</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>JNK Mitogen-Activated Protein Kinases (metabolism)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Proto-Oncogene Proteins (metabolism)</term>
<term>Proto-Oncogene Proteins c-akt</term>
<term>SARS Virus (pathogenicity)</term>
<term>Signal Transduction</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>JNK Mitogen-Activated Protein Kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Proto-Oncogene Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phosphatidylinositol 3-Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Proto-Oncogene Proteins c-akt</term>
<term>Signal Transduction</term>
<term>Vero Cells</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Persistence was established after most of the SARS-CoV-infected Vero E6 cells died. RNA of the defective interfering virus was not observed in the persistently infected cells by Northern blot analysis. SARS-CoV diluted to 2 PFU failed to establish persistence, suggesting that some particular viruses in the seed virus did not induce persistent infection. Interestingly, a viral receptor, angiotensin converting enzyme (ACE)-2, was down-regulated in persistently infected cells. G418-selected clones established from parent Vero E6 cells, which were transfected with a plasmid containing the neomycin resistance gene, were infected with SARS-CoV, resulting in a potential cell population capable of persistence in Vero E6 cells. Our previous studies demonstrated that signaling pathways of extracellular signal-related kinase (ERK1/2), c-Jun N-terminal protein kinase (JNK), p38 mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3'-kinase (PI3K)/Akt were activated in SARS-CoV-infected Vero E6 cells. Previous studies also showed that the activation of p38 MAPK by viral infection-induced apoptosis, and a weak activation of Akt was not sufficient to protect from apoptosis. In the present study, we showed that the inhibitors of JNK and PI3K/Akt inhibited the establishment of persistence, but those of MAPK/ERK kinase (MEK; as an inhibitor for ERK1/2) and p38 MAPK did not. These results indicated that two signaling pathways of JNK and PI3K/Akt were important for the establishment of persistence in Vero E6 cells.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15916886</PMID>
<DateCompleted><Year>2005</Year>
<Month>07</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN>
<JournalIssue CitedMedium="Print"><Volume>1741</Volume>
<Issue>1-2</Issue>
<PubDate><Year>2005</Year>
<Month>Jun</Month>
<Day>30</Day>
</PubDate>
</JournalIssue>
<Title>Biochimica et biophysica acta</Title>
<ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation>
</Journal>
<ArticleTitle>JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells.</ArticleTitle>
<Pagination><MedlinePgn>4-10</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Persistence was established after most of the SARS-CoV-infected Vero E6 cells died. RNA of the defective interfering virus was not observed in the persistently infected cells by Northern blot analysis. SARS-CoV diluted to 2 PFU failed to establish persistence, suggesting that some particular viruses in the seed virus did not induce persistent infection. Interestingly, a viral receptor, angiotensin converting enzyme (ACE)-2, was down-regulated in persistently infected cells. G418-selected clones established from parent Vero E6 cells, which were transfected with a plasmid containing the neomycin resistance gene, were infected with SARS-CoV, resulting in a potential cell population capable of persistence in Vero E6 cells. Our previous studies demonstrated that signaling pathways of extracellular signal-related kinase (ERK1/2), c-Jun N-terminal protein kinase (JNK), p38 mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3'-kinase (PI3K)/Akt were activated in SARS-CoV-infected Vero E6 cells. Previous studies also showed that the activation of p38 MAPK by viral infection-induced apoptosis, and a weak activation of Akt was not sufficient to protect from apoptosis. In the present study, we showed that the inhibitors of JNK and PI3K/Akt inhibited the establishment of persistence, but those of MAPK/ERK kinase (MEK; as an inhibitor for ERK1/2) and p38 MAPK did not. These results indicated that two signaling pathways of JNK and PI3K/Akt were important for the establishment of persistence in Vero E6 cells.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mizutani</LastName>
<ForeName>Tetsuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology 1, National Institute of Infectious Diseases, Musashimurayama, Tokyo 208-0011, Japan. tmizutan@nih.go.jp</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fukushi</LastName>
<ForeName>Shuetsu</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Saijo</LastName>
<ForeName>Masayuki</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kurane</LastName>
<ForeName>Ichiro</ForeName>
<Initials>I</Initials>
</Author>
<Author ValidYN="Y"><LastName>Morikawa</LastName>
<ForeName>Shigeru</ForeName>
<Initials>S</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>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Biochim Biophys Acta</MedlineTA>
<NlmUniqueID>0217513</NlmUniqueID>
<ISSNLinking>0006-3002</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011518">Proto-Oncogene Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D051057">Proto-Oncogene Proteins c-akt</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber>
<NameOfSubstance UI="D048031">JNK Mitogen-Activated Protein Kinases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D048031" MajorTopicYN="N">JNK Mitogen-Activated Protein Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011518" MajorTopicYN="N">Proto-Oncogene Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051057" MajorTopicYN="N">Proto-Oncogene Proteins c-akt</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year>
<Month>03</Month>
<Day>02</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2005</Year>
<Month>04</Month>
<Day>19</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2005</Year>
<Month>04</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2005</Year>
<Month>5</Month>
<Day>27</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2005</Year>
<Month>7</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2005</Year>
<Month>5</Month>
<Day>27</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">15916886</ArticleId>
<ArticleId IdType="pii">S0925-4439(05)00052-9</ArticleId>
<ArticleId IdType="doi">10.1016/j.bbadis.2005.04.004</ArticleId>
<ArticleId IdType="pmc">PMC7125767</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Proc Soc Exp Biol Med. 1966 Mar;121(3):976-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4956837</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1997 Apr;71(4):3255-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9060690</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1999 May 11;96(10):5533-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10318918</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2004 Oct 1;327(2):169-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15351204</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Jul 9;319(4):1228-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15194498</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Vet Med Sci. 1995 Oct;57(5):813-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8593285</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2002 Sep;76(18):9207-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12186904</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>FEBS Lett. 2004 Nov 5;577(1-2):187-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15527783</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Nov 28;311(4):870-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14623261</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1988 Jul;85(14):5259-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3134658</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem J. 2004 Oct 1;383(Pt 1):13-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15294014</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1988 Aug;62(8):2859-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3392771</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2002 Dec 20;304(2):415-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12504580</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2003 Nov 10;316(1):104-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14599795</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Microb Pathog. 1987 Oct;3(4):309-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2849022</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Med Virol. 2004 Sep;74(1):1-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15258961</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Microbiol Immunol. 2000;44(7):597-603</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10981833</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002716 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002716 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:15916886 |texte= JNK and PI3k/Akt signaling pathways are required for establishing persistent SARS-CoV infection in Vero E6 cells. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:15916886" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |