Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines.
Identifieur interne : 000739 ( PubMed/Corpus ); précédent : 000738; suivant : 000740Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines.
Auteurs : Diana Vester ; Erdmann Rapp ; Dörte Gade ; Yvonne Genzel ; Udo ReichlSource :
- Proteomics [ 1615-9861 ] ; 2009.
English descriptors
- KwdEn :
- Animals, Apoptosis (physiology), Cell Line, Cell Line, Tumor, Chromatography, High Pressure Liquid, Cytoskeletal Proteins (metabolism), Dogs, Electrophoresis, Gel, Two-Dimensional, Host-Pathogen Interactions, Humans, Influenza A Virus, H1N1 Subtype (immunology), Influenza A Virus, H1N1 Subtype (metabolism), Influenza A Virus, H1N1 Subtype (physiology), Influenza Vaccines (biosynthesis), Influenza, Human (metabolism), Influenza, Human (pathology), Influenza, Human (virology), Proteome (analysis), Proteome (metabolism), Proteomics (methods), Signal Transduction, Stress, Physiological, Tandem Mass Spectrometry.
- MESH :
- chemical , analysis : Proteome.
- chemical , biosynthesis : Influenza Vaccines.
- chemical , metabolism : Cytoskeletal Proteins, Proteome.
- immunology : Influenza A Virus, H1N1 Subtype.
- metabolism : Influenza A Virus, H1N1 Subtype, Influenza, Human.
- methods : Proteomics.
- pathology : Influenza, Human.
- physiology : Apoptosis, Influenza A Virus, H1N1 Subtype.
- virology : Influenza, Human.
- Animals, Cell Line, Cell Line, Tumor, Chromatography, High Pressure Liquid, Dogs, Electrophoresis, Gel, Two-Dimensional, Host-Pathogen Interactions, Humans, Signal Transduction, Stress, Physiological, Tandem Mass Spectrometry.
Abstract
Over the last years virus-host cell interactions were investigated in numerous studies. Viral strategies for evasion of innate immune response, inhibition of cellular protein synthesis and permission of viral RNA and protein production were disclosed. With quantitative proteome technology, comprehensive studies concerning the impact of viruses on the cellular machinery of their host cells at protein level are possible. Therefore, 2-D DIGE and nanoHPLC-nanoESI-MS/MS analysis were used to qualitatively and quantitatively determine the dynamic cellular proteome responses of two mammalian cell lines to human influenza A virus infection. A cell line used for vaccine production (MDCK) was compared with a human lung carcinoma cell line (A549) as a reference model. Analyzing 2-D gels of the proteomes of uninfected and influenza-infected host cells, 16 quantitatively altered protein spots (at least +/-1.7-fold change in relative abundance, p<0.001) were identified for both cell lines. Most significant changes were found for keratins, major components of the cytoskeleton system, and for Mx proteins, interferon-induced key components of the host cell defense. Time series analysis of infection processes allowed the identification of further proteins that are described to be involved in protein synthesis, signal transduction and apoptosis events. Most likely, these proteins are required for supporting functions during influenza viral life cycle or host cell stress response. Quantitative proteome-wide profiling of virus infection can provide insights into complexity and dynamics of virus-host cell interactions and may accelerate antiviral research and support optimization of vaccine manufacturing processes.
DOI: 10.1002/pmic.200800893
PubMed: 19504497
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pubmed:19504497Le document en format XML
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Reichl</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19504497</idno><idno type="pmid">19504497</idno><idno type="doi">10.1002/pmic.200800893</idno><idno type="wicri:Area/PubMed/Corpus">000739</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000739</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines.</title><author><name sortKey="Vester, Diana" sort="Vester, Diana" uniqKey="Vester D" first="Diana" last="Vester">Diana Vester</name><affiliation><nlm:affiliation>Bioprocess Engineering, Otto-von-Guericke-University Magdeburg, Magdeburg, Germany. vester@mpi-magdeburg.mpg.de</nlm:affiliation></affiliation></author><author><name sortKey="Rapp, Erdmann" sort="Rapp, Erdmann" uniqKey="Rapp E" first="Erdmann" 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qualifier="immunology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Proteomics</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Apoptosis</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cell Line, Tumor</term><term>Chromatography, High Pressure Liquid</term><term>Dogs</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Signal Transduction</term><term>Stress, Physiological</term><term>Tandem Mass Spectrometry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Over the last years virus-host cell interactions were investigated in numerous studies. Viral strategies for evasion of innate immune response, inhibition of cellular protein synthesis and permission of viral RNA and protein production were disclosed. With quantitative proteome technology, comprehensive studies concerning the impact of viruses on the cellular machinery of their host cells at protein level are possible. Therefore, 2-D DIGE and nanoHPLC-nanoESI-MS/MS analysis were used to qualitatively and quantitatively determine the dynamic cellular proteome responses of two mammalian cell lines to human influenza A virus infection. A cell line used for vaccine production (MDCK) was compared with a human lung carcinoma cell line (A549) as a reference model. Analyzing 2-D gels of the proteomes of uninfected and influenza-infected host cells, 16 quantitatively altered protein spots (at least +/-1.7-fold change in relative abundance, p<0.001) were identified for both cell lines. Most significant changes were found for keratins, major components of the cytoskeleton system, and for Mx proteins, interferon-induced key components of the host cell defense. Time series analysis of infection processes allowed the identification of further proteins that are described to be involved in protein synthesis, signal transduction and apoptosis events. Most likely, these proteins are required for supporting functions during influenza viral life cycle or host cell stress response. Quantitative proteome-wide profiling of virus infection can provide insights into complexity and dynamics of virus-host cell interactions and may accelerate antiviral research and support optimization of vaccine manufacturing processes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19504497</PMID><DateCompleted><Year>2009</Year><Month>09</Month><Day>25</Day></DateCompleted><DateRevised><Year>2009</Year><Month>07</Month><Day>06</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1615-9861</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>12</Issue><PubDate><Year>2009</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Proteomics</Title><ISOAbbreviation>Proteomics</ISOAbbreviation></Journal><ArticleTitle>Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines.</ArticleTitle><Pagination><MedlinePgn>3316-27</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/pmic.200800893</ELocationID><Abstract><AbstractText>Over the last years virus-host cell interactions were investigated in numerous studies. Viral strategies for evasion of innate immune response, inhibition of cellular protein synthesis and permission of viral RNA and protein production were disclosed. With quantitative proteome technology, comprehensive studies concerning the impact of viruses on the cellular machinery of their host cells at protein level are possible. Therefore, 2-D DIGE and nanoHPLC-nanoESI-MS/MS analysis were used to qualitatively and quantitatively determine the dynamic cellular proteome responses of two mammalian cell lines to human influenza A virus infection. A cell line used for vaccine production (MDCK) was compared with a human lung carcinoma cell line (A549) as a reference model. Analyzing 2-D gels of the proteomes of uninfected and influenza-infected host cells, 16 quantitatively altered protein spots (at least +/-1.7-fold change in relative abundance, p<0.001) were identified for both cell lines. Most significant changes were found for keratins, major components of the cytoskeleton system, and for Mx proteins, interferon-induced key components of the host cell defense. Time series analysis of infection processes allowed the identification of further proteins that are described to be involved in protein synthesis, signal transduction and apoptosis events. Most likely, these proteins are required for supporting functions during influenza viral life cycle or host cell stress response. Quantitative proteome-wide profiling of virus infection can provide insights into complexity and dynamics of virus-host cell interactions and may accelerate antiviral research and support optimization of vaccine manufacturing processes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vester</LastName><ForeName>Diana</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Bioprocess Engineering, Otto-von-Guericke-University Magdeburg, Magdeburg, Germany. vester@mpi-magdeburg.mpg.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rapp</LastName><ForeName>Erdmann</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Gade</LastName><ForeName>Dörte</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Genzel</LastName><ForeName>Yvonne</ForeName><Initials>Y</Initials></Author><Author 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MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003598" MajorTopicYN="N">Cytoskeletal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004285" MajorTopicYN="N">Dogs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015180" MajorTopicYN="N">Electrophoresis, Gel, Two-Dimensional</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" 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