Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells
Identifieur interne : 003295 ( Main/Exploration ); précédent : 003294; suivant : 003296Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells
Auteurs : Ning Liu [République populaire de Chine] ; Wenjun Song [République populaire de Chine] ; Pui Wang [République populaire de Chine] ; Kimchung Lee [République populaire de Chine] ; Wan Chan [République populaire de Chine] ; Honglin Chen [République populaire de Chine, Hong Kong] ; Zongwei Cai [République populaire de Chine, Hong Kong]Source :
- PROTEOMICS [ 1615-9853 ] ; 2008-05.
English descriptors
- Teeft :
- Actin, Actin analogs, Actin cytoskeleton, Actin tails, Avian influenza, Avian influenza virus, Binding activity, Biorad, Blot analysis, Cell line, Cellular, Cellular metabolism, Cellular proteins, Cellular responses, Chloride intracellular channel protein, Component subunit beta, Constant voltage, Cytokeratin, Cytokeratin type, Cytoplasmic, Cytoplasmic actin, Cytoskeletal, Cytoskeleton, Cytoskeleton components, Different time courses, Differentially, Donkey antimouse, Electrophoresis separation, Equilibration solution, Expression pattern, Full length, Gene transcription, Gmbh, Hong kong, Hong kong baptist university, Host cells, Human cell line, Human cells, Human origin, Image analysis, Indirect immunofluorescence, Infection process, Influenza, Influenza virus, Influenza viruses, Isomerase, Keratin, Kgaa, Mammalian cells, Mascot server, Mass spectra, Mass spectrometer, Matrix solution, Mdck cells, Microbiology proteomics, Molecular weight, Parent ions, Passive mode, Pdquest software, Peptide, Peptide tolerance, Plasma membrane, Positive identification, Possible role, Postinfection, Primary antibodies, Prohibitin, Protein, Protein spot, Protein spots, Protein synthesis, Proteins differentially, Proteomic analysis, Proteomic approaches, Proteomics, Pyruvate dehydrogenase, Rehydration solution, Ribosomal protein, Room temperature, Sequence coverage, Sodium thiosulfate, Theoretical values, Time course, Time point, Time points, Tryptic peptides, Vaccinia virus, Vacuum centrifuge, Verlag, Verlag gmbh, Viral, Viral studies, Virus, Virus infection, Virus particle internalization, Weinheim, Weinheim proteomics, Western blot analysis.
Abstract
We present the first proteomic analysis on the cellular responses to avian influenza virus (H9N2) infection in a human cell line in different time courses in order to search for target proteins for viral pathogenesis/adaptation studies. By using 2‐DE coupled with MALDI‐TOF MS and nano‐ESI‐MS/MS, we identified a set of differentially expressed cellular proteins, including cytoplasmic actin, cytokeratin, prohibitin, enoyl‐CoA hydratase, peptide‐prolyl cis–trans isomerase A (PPIase A), chloride intracellular channel protein 1, pyruvate dehydrogenase E1 component subunit beta, adenine phosphoribosyltransferase, guanine nucleotide‐binding protein subunit beta, nucleoside diphosphate kinase A, elongation factor 1‐beta and splicing factor, arginine/serine rich 1. The most significant changes in different time courses were found in cytoplasmic actin and cytokeratin, both of which constituted the major components of cytoskeleton network in the cells. The obtained data suggested a possible role of the cytoskeleton during avian influenza virus infection of mammalian cells, which might help for better understanding of the dynamics of avian influenza virus and host interaction in mammalian cell setting.
Url:
DOI: 10.1002/pmic.200700757
Affiliations:
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xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Chemistry, Hong Kong Baptist University, Hong Kong SAR</wicri:regionArea><wicri:noRegion>Hong Kong SAR</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Hong Kong</country></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">PROTEOMICS</title><title level="j" type="alt">PROTEOMICS</title><idno type="ISSN">1615-9853</idno><idno type="eISSN">1615-9861</idno><imprint><biblScope unit="vol">8</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="1851">1851</biblScope><biblScope unit="page" to="1858">1858</biblScope><biblScope unit="page-count">8</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2008-05">2008-05</date></imprint><idno type="ISSN">1615-9853</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1615-9853</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Actin</term><term>Actin analogs</term><term>Actin cytoskeleton</term><term>Actin tails</term><term>Avian influenza</term><term>Avian influenza virus</term><term>Binding activity</term><term>Biorad</term><term>Blot analysis</term><term>Cell line</term><term>Cellular</term><term>Cellular metabolism</term><term>Cellular proteins</term><term>Cellular responses</term><term>Chloride intracellular channel protein</term><term>Component subunit beta</term><term>Constant voltage</term><term>Cytokeratin</term><term>Cytokeratin type</term><term>Cytoplasmic</term><term>Cytoplasmic actin</term><term>Cytoskeletal</term><term>Cytoskeleton</term><term>Cytoskeleton components</term><term>Different time courses</term><term>Differentially</term><term>Donkey antimouse</term><term>Electrophoresis separation</term><term>Equilibration solution</term><term>Expression pattern</term><term>Full length</term><term>Gene transcription</term><term>Gmbh</term><term>Hong kong</term><term>Hong kong baptist university</term><term>Host cells</term><term>Human cell line</term><term>Human cells</term><term>Human origin</term><term>Image analysis</term><term>Indirect immunofluorescence</term><term>Infection process</term><term>Influenza</term><term>Influenza virus</term><term>Influenza viruses</term><term>Isomerase</term><term>Keratin</term><term>Kgaa</term><term>Mammalian cells</term><term>Mascot server</term><term>Mass spectra</term><term>Mass spectrometer</term><term>Matrix solution</term><term>Mdck cells</term><term>Microbiology proteomics</term><term>Molecular weight</term><term>Parent ions</term><term>Passive mode</term><term>Pdquest software</term><term>Peptide</term><term>Peptide tolerance</term><term>Plasma membrane</term><term>Positive identification</term><term>Possible role</term><term>Postinfection</term><term>Primary antibodies</term><term>Prohibitin</term><term>Protein</term><term>Protein spot</term><term>Protein spots</term><term>Protein synthesis</term><term>Proteins differentially</term><term>Proteomic analysis</term><term>Proteomic approaches</term><term>Proteomics</term><term>Pyruvate dehydrogenase</term><term>Rehydration solution</term><term>Ribosomal protein</term><term>Room temperature</term><term>Sequence coverage</term><term>Sodium thiosulfate</term><term>Theoretical values</term><term>Time course</term><term>Time point</term><term>Time points</term><term>Tryptic peptides</term><term>Vaccinia virus</term><term>Vacuum centrifuge</term><term>Verlag</term><term>Verlag gmbh</term><term>Viral</term><term>Viral studies</term><term>Virus</term><term>Virus infection</term><term>Virus particle internalization</term><term>Weinheim</term><term>Weinheim proteomics</term><term>Western blot analysis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We present the first proteomic analysis on the cellular responses to avian influenza virus (H9N2) infection in a human cell line in different time courses in order to search for target proteins for viral pathogenesis/adaptation studies. By using 2‐DE coupled with MALDI‐TOF MS and nano‐ESI‐MS/MS, we identified a set of differentially expressed cellular proteins, including cytoplasmic actin, cytokeratin, prohibitin, enoyl‐CoA hydratase, peptide‐prolyl cis–trans isomerase A (PPIase A), chloride intracellular channel protein 1, pyruvate dehydrogenase E1 component subunit beta, adenine phosphoribosyltransferase, guanine nucleotide‐binding protein subunit beta, nucleoside diphosphate kinase A, elongation factor 1‐beta and splicing factor, arginine/serine rich 1. The most significant changes in different time courses were found in cytoplasmic actin and cytokeratin, both of which constituted the major components of cytoskeleton network in the cells. The obtained data suggested a possible role of the cytoskeleton during avian influenza virus infection of mammalian cells, which might help for better understanding of the dynamics of avian influenza virus and host interaction in mammalian cell setting.</div></front></TEI><affiliations><list><country><li>Hong Kong</li><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Liu, Ning" sort="Liu, Ning" uniqKey="Liu N" first="Ning" last="Liu">Ning Liu</name></noRegion><name sortKey="Cai, Zongwei" sort="Cai, Zongwei" uniqKey="Cai Z" first="Zongwei" last="Cai">Zongwei Cai</name><name sortKey="Chan, Wan" sort="Chan, Wan" uniqKey="Chan W" first="Wan" last="Chan">Wan Chan</name><name sortKey="Chen, Honglin" sort="Chen, Honglin" uniqKey="Chen H" first="Honglin" last="Chen">Honglin Chen</name><name sortKey="Lee, Kimchung" sort="Lee, Kimchung" uniqKey="Lee K" first="Kimchung" last="Lee">Kimchung Lee</name><name sortKey="Song, Wenjun" sort="Song, Wenjun" uniqKey="Song W" first="Wenjun" last="Song">Wenjun Song</name><name sortKey="Wang, Pui" sort="Wang, Pui" uniqKey="Wang P" first="Pui" last="Wang">Pui Wang</name></country><country name="Hong Kong"><noRegion><name sortKey="Chen, Honglin" sort="Chen, Honglin" uniqKey="Chen H" first="Honglin" last="Chen">Honglin Chen</name></noRegion><name sortKey="Cai, Zongwei" sort="Cai, Zongwei" uniqKey="Cai Z" first="Zongwei" last="Cai">Zongwei Cai</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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