HSPB1 is an intracellular antiviral factor against hepatitis B virus
Hepatitis B virus (HBV) is the most common of the hepatitis viruses that cause chronic liver infections in humans and it is considered a major global health problem. However, the mechanisms of HBV replication are complex and not yet fully understood. In this study, the HBV DNA‐transfected HepG2.2.15...
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| Veröffentlicht in: | Journal of cellular biochemistry 2013-01, Vol.114 (1), p.162-173 |
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| creator | Tong, Shi-Wen Yang, Yi-Xuan Hu, Huai-Dong An, Xuan Ye, Feng Ren, Hong Li, Sang-Lin Zhang, Da-Zhi |
| description | Hepatitis B virus (HBV) is the most common of the hepatitis viruses that cause chronic liver infections in humans and it is considered a major global health problem. However, the mechanisms of HBV replication are complex and not yet fully understood. In this study, the HBV DNA‐transfected HepG2.2.15 cell line and its parental HepG2 cell line were analyzed by isobaric tags for relative and absolute quantitation (iTRAQ)‐coupled two‐dimensional liquid chromatography tandem mass‐spectrophotometry (2D LC‐MS/MS), a successfully exploited high‐throughput proteomic technology. In total, 2,028 unique proteins were identified and 170 proteins were differentially expressed in HepG2.2.15 cells as compared with that in HepG2. Several differentially expressed proteins were further validated by Western blot and real‐time quantitative reverse transcription‐PCR. Furthermore, the association of HBV replication with heat shock protein B1, one of the highly expressed proteins in HepG2.2.15 cells, was verified. HSPB1 functions as a anti‐viral protein during HBV infection by specifically inducing type interferon and some downstream antiviral effectors. This study is the first to report the application of iTRAQ technology to analyze the underlying mechanisms of HBV replication. Many of the differentially expressed proteins identified have not been linked to HBV replication before, and may provide valuable novel insights into HBV replication. J. Cell. Biochem. 114: 162–173, 2012. © 2012 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/jcb.24313 |
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However, the mechanisms of HBV replication are complex and not yet fully understood. In this study, the HBV DNA‐transfected HepG2.2.15 cell line and its parental HepG2 cell line were analyzed by isobaric tags for relative and absolute quantitation (iTRAQ)‐coupled two‐dimensional liquid chromatography tandem mass‐spectrophotometry (2D LC‐MS/MS), a successfully exploited high‐throughput proteomic technology. In total, 2,028 unique proteins were identified and 170 proteins were differentially expressed in HepG2.2.15 cells as compared with that in HepG2. Several differentially expressed proteins were further validated by Western blot and real‐time quantitative reverse transcription‐PCR. Furthermore, the association of HBV replication with heat shock protein B1, one of the highly expressed proteins in HepG2.2.15 cells, was verified. HSPB1 functions as a anti‐viral protein during HBV infection by specifically inducing type interferon and some downstream antiviral effectors. This study is the first to report the application of iTRAQ technology to analyze the underlying mechanisms of HBV replication. Many of the differentially expressed proteins identified have not been linked to HBV replication before, and may provide valuable novel insights into HBV replication. J. Cell. Biochem. 114: 162–173, 2012. © 2012 Wiley Periodicals, Inc.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/jcb.24313</identifier><identifier>PMID: 22887120</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Sequence ; Chromatography, Liquid - methods ; Gene Expression ; Gene Expression Profiling ; Genetic Vectors ; Hep G2 Cells - immunology ; Hep G2 Cells - metabolism ; Hep G2 Cells - virology ; Hepatitis B e Antigens - genetics ; Hepatitis B e Antigens - metabolism ; Hepatitis B Surface Antigens - genetics ; Hepatitis B Surface Antigens - metabolism ; HEPATITIS B VIRUS ; Hepatitis B virus - physiology ; Host-Pathogen Interactions ; HSP27 Heat-Shock Proteins - genetics ; HSP27 Heat-Shock Proteins - metabolism ; HSPB1 ; Humans ; Interferon Type I - biosynthesis ; Interferon Type I - immunology ; iTRAQ ; Molecular Sequence Data ; Proteomics ; Tandem Mass Spectrometry - methods ; Transcriptome ; Transfection ; Virus Replication - physiology</subject><ispartof>Journal of cellular biochemistry, 2013-01, Vol.114 (1), p.162-173</ispartof><rights>Copyright © 2012 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4263-e1c0b90814ad87661811fffc2906fa186ea173172187a3feab36cf0c0c1a60fc3</citedby><cites>FETCH-LOGICAL-c4263-e1c0b90814ad87661811fffc2906fa186ea173172187a3feab36cf0c0c1a60fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcb.24313$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcb.24313$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22887120$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tong, Shi-Wen</creatorcontrib><creatorcontrib>Yang, Yi-Xuan</creatorcontrib><creatorcontrib>Hu, Huai-Dong</creatorcontrib><creatorcontrib>An, Xuan</creatorcontrib><creatorcontrib>Ye, Feng</creatorcontrib><creatorcontrib>Ren, Hong</creatorcontrib><creatorcontrib>Li, Sang-Lin</creatorcontrib><creatorcontrib>Zhang, Da-Zhi</creatorcontrib><title>HSPB1 is an intracellular antiviral factor against hepatitis B virus</title><title>Journal of cellular biochemistry</title><addtitle>J. Cell. Biochem</addtitle><description>Hepatitis B virus (HBV) is the most common of the hepatitis viruses that cause chronic liver infections in humans and it is considered a major global health problem. However, the mechanisms of HBV replication are complex and not yet fully understood. In this study, the HBV DNA‐transfected HepG2.2.15 cell line and its parental HepG2 cell line were analyzed by isobaric tags for relative and absolute quantitation (iTRAQ)‐coupled two‐dimensional liquid chromatography tandem mass‐spectrophotometry (2D LC‐MS/MS), a successfully exploited high‐throughput proteomic technology. In total, 2,028 unique proteins were identified and 170 proteins were differentially expressed in HepG2.2.15 cells as compared with that in HepG2. Several differentially expressed proteins were further validated by Western blot and real‐time quantitative reverse transcription‐PCR. Furthermore, the association of HBV replication with heat shock protein B1, one of the highly expressed proteins in HepG2.2.15 cells, was verified. HSPB1 functions as a anti‐viral protein during HBV infection by specifically inducing type interferon and some downstream antiviral effectors. This study is the first to report the application of iTRAQ technology to analyze the underlying mechanisms of HBV replication. Many of the differentially expressed proteins identified have not been linked to HBV replication before, and may provide valuable novel insights into HBV replication. J. Cell. Biochem. 114: 162–173, 2012. © 2012 Wiley Periodicals, Inc.</description><subject>Amino Acid Sequence</subject><subject>Chromatography, Liquid - methods</subject><subject>Gene Expression</subject><subject>Gene Expression Profiling</subject><subject>Genetic Vectors</subject><subject>Hep G2 Cells - immunology</subject><subject>Hep G2 Cells - metabolism</subject><subject>Hep G2 Cells - virology</subject><subject>Hepatitis B e Antigens - genetics</subject><subject>Hepatitis B e Antigens - metabolism</subject><subject>Hepatitis B Surface Antigens - genetics</subject><subject>Hepatitis B Surface Antigens - metabolism</subject><subject>HEPATITIS B VIRUS</subject><subject>Hepatitis B virus - physiology</subject><subject>Host-Pathogen Interactions</subject><subject>HSP27 Heat-Shock Proteins - genetics</subject><subject>HSP27 Heat-Shock Proteins - metabolism</subject><subject>HSPB1</subject><subject>Humans</subject><subject>Interferon Type I - biosynthesis</subject><subject>Interferon Type I - immunology</subject><subject>iTRAQ</subject><subject>Molecular Sequence Data</subject><subject>Proteomics</subject><subject>Tandem Mass Spectrometry - methods</subject><subject>Transcriptome</subject><subject>Transfection</subject><subject>Virus Replication - physiology</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10MFu1DAQBmCrArVL4dAXqCJxKYe0M3ZiO0c2pS1oBUgUIXGxZl279ZJNtnYC9O1x2bYHJE4jjb75NfoZO0A4RgB-srLLY14JFDtshtCospJV9YzNQAkouUC-x16ktAKAphF8l-1xrrVCDjN2evHl8xyLkArqi9CPkazruqmjmBdj-BkidYUnOw55cU2hT2Nx4zY0hjHfzIsMpvSSPffUJffqYe6zr2fvLtuLcvHp_H37dlHaiktROrSwbEBjRVdaSYka0XtveQPSE2rpCJVAxVErEt7RUkjrwYJFkuCt2GdH29xNHG4nl0azDun-X-rdMCWDqLTUkiud6et_6GqYYp-_y6rGpq6aWmT1ZqtsHFKKzptNDGuKdwbB3FdrcrXmb7XZHj4kTsu1u3qSj11mcLIFv0Ln7v6fZD6088fIcnsR0uh-P11Q_GGkEqo23z6em_ZM1Zf14rtpxR-1to9g</recordid><startdate>201301</startdate><enddate>201301</enddate><creator>Tong, Shi-Wen</creator><creator>Yang, Yi-Xuan</creator><creator>Hu, Huai-Dong</creator><creator>An, Xuan</creator><creator>Ye, Feng</creator><creator>Ren, Hong</creator><creator>Li, Sang-Lin</creator><creator>Zhang, Da-Zhi</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201301</creationdate><title>HSPB1 is an intracellular antiviral factor against hepatitis B virus</title><author>Tong, Shi-Wen ; Yang, Yi-Xuan ; Hu, Huai-Dong ; An, Xuan ; Ye, Feng ; Ren, Hong ; Li, Sang-Lin ; Zhang, Da-Zhi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4263-e1c0b90814ad87661811fffc2906fa186ea173172187a3feab36cf0c0c1a60fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Chromatography, Liquid - methods</topic><topic>Gene Expression</topic><topic>Gene Expression Profiling</topic><topic>Genetic Vectors</topic><topic>Hep G2 Cells - immunology</topic><topic>Hep G2 Cells - metabolism</topic><topic>Hep G2 Cells - virology</topic><topic>Hepatitis B e Antigens - genetics</topic><topic>Hepatitis B e Antigens - metabolism</topic><topic>Hepatitis B Surface Antigens - genetics</topic><topic>Hepatitis B Surface Antigens - metabolism</topic><topic>HEPATITIS B VIRUS</topic><topic>Hepatitis B virus - physiology</topic><topic>Host-Pathogen Interactions</topic><topic>HSP27 Heat-Shock Proteins - genetics</topic><topic>HSP27 Heat-Shock Proteins - metabolism</topic><topic>HSPB1</topic><topic>Humans</topic><topic>Interferon Type I - biosynthesis</topic><topic>Interferon Type I - immunology</topic><topic>iTRAQ</topic><topic>Molecular Sequence Data</topic><topic>Proteomics</topic><topic>Tandem Mass Spectrometry - methods</topic><topic>Transcriptome</topic><topic>Transfection</topic><topic>Virus Replication - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tong, Shi-Wen</creatorcontrib><creatorcontrib>Yang, Yi-Xuan</creatorcontrib><creatorcontrib>Hu, Huai-Dong</creatorcontrib><creatorcontrib>An, Xuan</creatorcontrib><creatorcontrib>Ye, Feng</creatorcontrib><creatorcontrib>Ren, Hong</creatorcontrib><creatorcontrib>Li, Sang-Lin</creatorcontrib><creatorcontrib>Zhang, Da-Zhi</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tong, Shi-Wen</au><au>Yang, Yi-Xuan</au><au>Hu, Huai-Dong</au><au>An, Xuan</au><au>Ye, Feng</au><au>Ren, Hong</au><au>Li, Sang-Lin</au><au>Zhang, Da-Zhi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HSPB1 is an intracellular antiviral factor against hepatitis B virus</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J. Cell. Biochem</addtitle><date>2013-01</date><risdate>2013</risdate><volume>114</volume><issue>1</issue><spage>162</spage><epage>173</epage><pages>162-173</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><abstract>Hepatitis B virus (HBV) is the most common of the hepatitis viruses that cause chronic liver infections in humans and it is considered a major global health problem. However, the mechanisms of HBV replication are complex and not yet fully understood. In this study, the HBV DNA‐transfected HepG2.2.15 cell line and its parental HepG2 cell line were analyzed by isobaric tags for relative and absolute quantitation (iTRAQ)‐coupled two‐dimensional liquid chromatography tandem mass‐spectrophotometry (2D LC‐MS/MS), a successfully exploited high‐throughput proteomic technology. In total, 2,028 unique proteins were identified and 170 proteins were differentially expressed in HepG2.2.15 cells as compared with that in HepG2. Several differentially expressed proteins were further validated by Western blot and real‐time quantitative reverse transcription‐PCR. Furthermore, the association of HBV replication with heat shock protein B1, one of the highly expressed proteins in HepG2.2.15 cells, was verified. HSPB1 functions as a anti‐viral protein during HBV infection by specifically inducing type interferon and some downstream antiviral effectors. This study is the first to report the application of iTRAQ technology to analyze the underlying mechanisms of HBV replication. Many of the differentially expressed proteins identified have not been linked to HBV replication before, and may provide valuable novel insights into HBV replication. J. Cell. Biochem. 114: 162–173, 2012. © 2012 Wiley Periodicals, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>22887120</pmid><doi>10.1002/jcb.24313</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Chromatography, Liquid - methods Gene Expression Gene Expression Profiling Genetic Vectors Hep G2 Cells - immunology Hep G2 Cells - metabolism Hep G2 Cells - virology Hepatitis B e Antigens - genetics Hepatitis B e Antigens - metabolism Hepatitis B Surface Antigens - genetics Hepatitis B Surface Antigens - metabolism HEPATITIS B VIRUS Hepatitis B virus - physiology Host-Pathogen Interactions HSP27 Heat-Shock Proteins - genetics HSP27 Heat-Shock Proteins - metabolism HSPB1 Humans Interferon Type I - biosynthesis Interferon Type I - immunology iTRAQ Molecular Sequence Data Proteomics Tandem Mass Spectrometry - methods Transcriptome Transfection Virus Replication - physiology |
| title | HSPB1 is an intracellular antiviral factor against hepatitis B virus |
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