Monoubiquitinated Histone H1B Is Required for Antiviral Protection in CD4+T Cells Resistant to HIV-1
Linker histone H1B (H1B) coeluted with an antiviral activity during the purification of HIV-1 resistance factor (HRF) from supernatants of HRF(+) cells. Western blot analysis of the supernatant using α-H1 and α-ubiquitin antibodies detected the same band of roughly 46 kDa; this band was absent from...
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| Veröffentlicht in: | Biochemistry (Easton) 2004-12, Vol.43 (51), p.16203-16211 |
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| container_issue | 51 |
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| container_title | Biochemistry (Easton) |
| container_volume | 43 |
| creator | Lesner, Adam Kartvelishvili, Alex Lesniak, Jakob Nikolov, Dimitar Kartvelishvili, Magdalena Trillo-Pazos, Gusta Zablotna, Ewa Simm, Malgorzata |
| description | Linker histone H1B (H1B) coeluted with an antiviral activity during the purification of HIV-1 resistance factor (HRF) from supernatants of HRF(+) cells. Western blot analysis of the supernatant using α-H1 and α-ubiquitin antibodies detected the same band of roughly 46 kDa; this band was absent from the control supernatant. Depletion of histone from biologically active material did not affect its potential, suggesting that ubiquitinated H1B is not required for the HRF-mediated antiviral protection in HIV-1 susceptible target cells; however, specific silencing of histone H1B via RNAi in HRF(+) cells reduced the biological activity of cell culture supernatants by 96% and reversed the HIV-1 resistance phenotype of HRF(+) cells. Exposure to HRF induced ubiquitination and secretion of H1B from target HIV-1 susceptible cells, suggesting that ubiquitinated H1B is a cofactor of HRF, possibly regulating its expression and secretion from CD4+T cells induced to resist HIV-1 infection. |
| doi_str_mv | 10.1021/bi0492758 |
| format | Article |
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Western blot analysis of the supernatant using α-H1 and α-ubiquitin antibodies detected the same band of roughly 46 kDa; this band was absent from the control supernatant. Depletion of histone from biologically active material did not affect its potential, suggesting that ubiquitinated H1B is not required for the HRF-mediated antiviral protection in HIV-1 susceptible target cells; however, specific silencing of histone H1B via RNAi in HRF(+) cells reduced the biological activity of cell culture supernatants by 96% and reversed the HIV-1 resistance phenotype of HRF(+) cells. Exposure to HRF induced ubiquitination and secretion of H1B from target HIV-1 susceptible cells, suggesting that ubiquitinated H1B is a cofactor of HRF, possibly regulating its expression and secretion from CD4+T cells induced to resist HIV-1 infection.</description><identifier>ISSN: 0006-2960</identifier><identifier>ISSN: 0921-5093</identifier><identifier>EISSN: 1520-4995</identifier><identifier>EISSN: 1873-4936</identifier><identifier>DOI: 10.1021/bi0492758</identifier><identifier>PMID: 15610014</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>60 APPLIED LIFE SCIENCES ; AIDS VIRUS ; BIOLOGICAL FUNCTIONS ; CD4-Positive T-Lymphocytes - immunology ; CD4-Positive T-Lymphocytes - metabolism ; Chromatography, Ion Exchange ; HISTONES ; Histones - immunology ; Histones - isolation & purification ; Histones - metabolism ; HIV Infections - immunology ; HIV Infections - metabolism ; HIV-1 - immunology ; Humans ; Immunity, Innate - immunology ; national synchrotron light source ; T-Lymphocyte Subsets - immunology ; T-Lymphocyte Subsets - metabolism ; Ubiquitin - metabolism</subject><ispartof>Biochemistry (Easton), 2004-12, Vol.43 (51), p.16203-16211</ispartof><rights>Copyright © 2004 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a307t-7be36230f46c2205276fef904402aa77d687d31b2655316faa146fe58250ba213</citedby><cites>FETCH-LOGICAL-a307t-7be36230f46c2205276fef904402aa77d687d31b2655316faa146fe58250ba213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi0492758$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi0492758$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15610014$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/884243$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Lesner, Adam</creatorcontrib><creatorcontrib>Kartvelishvili, Alex</creatorcontrib><creatorcontrib>Lesniak, Jakob</creatorcontrib><creatorcontrib>Nikolov, Dimitar</creatorcontrib><creatorcontrib>Kartvelishvili, Magdalena</creatorcontrib><creatorcontrib>Trillo-Pazos, Gusta</creatorcontrib><creatorcontrib>Zablotna, Ewa</creatorcontrib><creatorcontrib>Simm, Malgorzata</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source (NSLS)</creatorcontrib><title>Monoubiquitinated Histone H1B Is Required for Antiviral Protection in CD4+T Cells Resistant to HIV-1</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Linker histone H1B (H1B) coeluted with an antiviral activity during the purification of HIV-1 resistance factor (HRF) from supernatants of HRF(+) cells. Western blot analysis of the supernatant using α-H1 and α-ubiquitin antibodies detected the same band of roughly 46 kDa; this band was absent from the control supernatant. Depletion of histone from biologically active material did not affect its potential, suggesting that ubiquitinated H1B is not required for the HRF-mediated antiviral protection in HIV-1 susceptible target cells; however, specific silencing of histone H1B via RNAi in HRF(+) cells reduced the biological activity of cell culture supernatants by 96% and reversed the HIV-1 resistance phenotype of HRF(+) cells. Exposure to HRF induced ubiquitination and secretion of H1B from target HIV-1 susceptible cells, suggesting that ubiquitinated H1B is a cofactor of HRF, possibly regulating its expression and secretion from CD4+T cells induced to resist HIV-1 infection.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>AIDS VIRUS</subject><subject>BIOLOGICAL FUNCTIONS</subject><subject>CD4-Positive T-Lymphocytes - immunology</subject><subject>CD4-Positive T-Lymphocytes - metabolism</subject><subject>Chromatography, Ion Exchange</subject><subject>HISTONES</subject><subject>Histones - immunology</subject><subject>Histones - isolation & purification</subject><subject>Histones - metabolism</subject><subject>HIV Infections - immunology</subject><subject>HIV Infections - metabolism</subject><subject>HIV-1 - immunology</subject><subject>Humans</subject><subject>Immunity, Innate - immunology</subject><subject>national synchrotron light source</subject><subject>T-Lymphocyte Subsets - immunology</subject><subject>T-Lymphocyte Subsets - metabolism</subject><subject>Ubiquitin - metabolism</subject><issn>0006-2960</issn><issn>0921-5093</issn><issn>1520-4995</issn><issn>1873-4936</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1u1DAUhS1ERYfCghdAZgESqgLX_8mypKUzqBVVGX7ExnISR7idsVvbQfD2dZVR2bCy7Pv53KMPoRcE3hGg5H3ngDdUifoRWhBBoeJNIx6jBQDIijYS9tHTlK7KlYPiT9A-EZIAEL5Aw3nwYerc7eSy8ybbAS9dysFbvCQf8CrhS1tmsbyPIeIjn91vF80GX8SQbZ9d8Nh53B7zwzVu7WZz_yGVBOMzzgEvV98q8gztjWaT7PPdeYC-fjxZt8vq7PPpqj06qwwDlSvVWSYpg5HLnlIQVMnRjg1wDtQYpQZZq4GRjkohGJGjMYQXQtRUQGcoYQfo1ZwbUnY69a40_NUH70tRXdecclaYNzNzE8PtZFPWW5f6Utx4G6akpSK1bBpewLcz2MeQUrSjvolua-JfTUDfa9cP2gv7chc6dVs7_CN3ngtQzUAxY_88zE28LguZEnp98UWfX7L2x_dPa_2z8K9n3vRJX4Up-uLtP4vvALOxlQ0</recordid><startdate>20041228</startdate><enddate>20041228</enddate><creator>Lesner, Adam</creator><creator>Kartvelishvili, Alex</creator><creator>Lesniak, Jakob</creator><creator>Nikolov, Dimitar</creator><creator>Kartvelishvili, Magdalena</creator><creator>Trillo-Pazos, Gusta</creator><creator>Zablotna, Ewa</creator><creator>Simm, Malgorzata</creator><general>American Chemical Society</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>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20041228</creationdate><title>Monoubiquitinated Histone H1B Is Required for Antiviral Protection in CD4+T Cells Resistant to HIV-1</title><author>Lesner, Adam ; Kartvelishvili, Alex ; Lesniak, Jakob ; Nikolov, Dimitar ; Kartvelishvili, Magdalena ; Trillo-Pazos, Gusta ; Zablotna, Ewa ; Simm, Malgorzata</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a307t-7be36230f46c2205276fef904402aa77d687d31b2655316faa146fe58250ba213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>AIDS VIRUS</topic><topic>BIOLOGICAL FUNCTIONS</topic><topic>CD4-Positive T-Lymphocytes - immunology</topic><topic>CD4-Positive T-Lymphocytes - metabolism</topic><topic>Chromatography, Ion Exchange</topic><topic>HISTONES</topic><topic>Histones - immunology</topic><topic>Histones - isolation & purification</topic><topic>Histones - metabolism</topic><topic>HIV Infections - immunology</topic><topic>HIV Infections - metabolism</topic><topic>HIV-1 - immunology</topic><topic>Humans</topic><topic>Immunity, Innate - immunology</topic><topic>national synchrotron light source</topic><topic>T-Lymphocyte Subsets - immunology</topic><topic>T-Lymphocyte Subsets - metabolism</topic><topic>Ubiquitin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lesner, Adam</creatorcontrib><creatorcontrib>Kartvelishvili, Alex</creatorcontrib><creatorcontrib>Lesniak, Jakob</creatorcontrib><creatorcontrib>Nikolov, Dimitar</creatorcontrib><creatorcontrib>Kartvelishvili, Magdalena</creatorcontrib><creatorcontrib>Trillo-Pazos, Gusta</creatorcontrib><creatorcontrib>Zablotna, Ewa</creatorcontrib><creatorcontrib>Simm, Malgorzata</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source (NSLS)</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>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lesner, Adam</au><au>Kartvelishvili, Alex</au><au>Lesniak, Jakob</au><au>Nikolov, Dimitar</au><au>Kartvelishvili, Magdalena</au><au>Trillo-Pazos, Gusta</au><au>Zablotna, Ewa</au><au>Simm, Malgorzata</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source (NSLS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoubiquitinated Histone H1B Is Required for Antiviral Protection in CD4+T Cells Resistant to HIV-1</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2004-12-28</date><risdate>2004</risdate><volume>43</volume><issue>51</issue><spage>16203</spage><epage>16211</epage><pages>16203-16211</pages><issn>0006-2960</issn><issn>0921-5093</issn><eissn>1520-4995</eissn><eissn>1873-4936</eissn><abstract>Linker histone H1B (H1B) coeluted with an antiviral activity during the purification of HIV-1 resistance factor (HRF) from supernatants of HRF(+) cells. Western blot analysis of the supernatant using α-H1 and α-ubiquitin antibodies detected the same band of roughly 46 kDa; this band was absent from the control supernatant. Depletion of histone from biologically active material did not affect its potential, suggesting that ubiquitinated H1B is not required for the HRF-mediated antiviral protection in HIV-1 susceptible target cells; however, specific silencing of histone H1B via RNAi in HRF(+) cells reduced the biological activity of cell culture supernatants by 96% and reversed the HIV-1 resistance phenotype of HRF(+) cells. Exposure to HRF induced ubiquitination and secretion of H1B from target HIV-1 susceptible cells, suggesting that ubiquitinated H1B is a cofactor of HRF, possibly regulating its expression and secretion from CD4+T cells induced to resist HIV-1 infection.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>15610014</pmid><doi>10.1021/bi0492758</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 2004-12, Vol.43 (51), p.16203-16211 |
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| source | ACS Publications; MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 60 APPLIED LIFE SCIENCES AIDS VIRUS BIOLOGICAL FUNCTIONS CD4-Positive T-Lymphocytes - immunology CD4-Positive T-Lymphocytes - metabolism Chromatography, Ion Exchange HISTONES Histones - immunology Histones - isolation & purification Histones - metabolism HIV Infections - immunology HIV Infections - metabolism HIV-1 - immunology Humans Immunity, Innate - immunology national synchrotron light source T-Lymphocyte Subsets - immunology T-Lymphocyte Subsets - metabolism Ubiquitin - metabolism |
| title | Monoubiquitinated Histone H1B Is Required for Antiviral Protection in CD4+T Cells Resistant to HIV-1 |
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