Role for the shelterin protein TRF2 in human herpesvirus 6A/B chromosomal integration
Human herpesviruses 6A and 6B (HHV-6A/B) are unique among human herpesviruses in their ability to integrate their genome into host chromosomes. Viral integration occurs at the ends of chromosomes within the host telomeres. The ends of the HHV-6A/B genomes contain telomeric repeats that facilitate th...
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| creator | Gilbert-Girard, Shella Gravel, Annie Collin, Vanessa Wight, Darren J Kaufer, Benedikt B Lazzerini-Denchi, Eros Flamand, Louis |
| description | Human herpesviruses 6A and 6B (HHV-6A/B) are unique among human herpesviruses in their ability to integrate their genome into host chromosomes. Viral integration occurs at the ends of chromosomes within the host telomeres. The ends of the HHV-6A/B genomes contain telomeric repeats that facilitate the integration process. Here, we report that productive infections are associated with a massive increase in telomeric sequences of viral origin. The majority of the viral telomeric signals can be detected within viral replication compartments (VRC) that contain the viral DNA processivity factor p41 and the viral immediate-early 2 (IE2) protein. Components of the shelterin protein complex present at telomeres, including TRF1 and TRF2 are also recruited to VRC during infection. Biochemical, immunofluorescence coupled with in situ hybridization and chromatin immunoprecipitation demonstrated the binding of TRF2 to the HHV-6A/B telomeric repeats. In addition, approximately 60% of the viral IE2 protein localize at cellular telomeres during infection. Transient knockdown of TRF2 resulted in greatly reduced (13%) localization of IE2 at cellular telomeres (p |
| doi_str_mv | 10.1371/journal.ppat.1008496 |
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Viral integration occurs at the ends of chromosomes within the host telomeres. The ends of the HHV-6A/B genomes contain telomeric repeats that facilitate the integration process. Here, we report that productive infections are associated with a massive increase in telomeric sequences of viral origin. The majority of the viral telomeric signals can be detected within viral replication compartments (VRC) that contain the viral DNA processivity factor p41 and the viral immediate-early 2 (IE2) protein. Components of the shelterin protein complex present at telomeres, including TRF1 and TRF2 are also recruited to VRC during infection. Biochemical, immunofluorescence coupled with in situ hybridization and chromatin immunoprecipitation demonstrated the binding of TRF2 to the HHV-6A/B telomeric repeats. In addition, approximately 60% of the viral IE2 protein localize at cellular telomeres during infection. Transient knockdown of TRF2 resulted in greatly reduced (13%) localization of IE2 at cellular telomeres (p<0.0001). Lastly, TRF2 knockdown reduced HHV-6A/B integration frequency (p<0.05), while no effect was observed on the infection efficiency. Overall, our study identified that HHV-6A/B IE2 localizes to telomeres during infection and highlight the role of TRF2 in HHV-6A/B infection and chromosomal integration.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1008496</identifier><identifier>PMID: 32320442</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Angina pectoris ; Antibodies ; Ataxia ; Biology and Life Sciences ; Cell division ; Chromatin ; Chromosomes ; Deoxyribonucleic acid ; DNA ; DNA damage ; EDTA ; Fluorescent antibody technique ; Genomes ; Genomics ; Health aspects ; Herpes viruses ; Herpesviruses ; Human performance ; Hybridization ; IE2 protein ; Immunofluorescence ; Immunoprecipitation ; Infection ; Infections ; Infectious diseases ; Integration ; Localization ; Medical research ; Plasmids ; Proteins ; Research and Analysis Methods ; Telomerase ; Telomere-binding protein ; Telomeres ; TRF2 protein ; Virus replication</subject><ispartof>PLoS pathogens, 2020-04, Vol.16 (4), p.e1008496-e1008496</ispartof><rights>COPYRIGHT 2020 Public Library of Science</rights><rights>This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication: https://creativecommons.org/publicdomain/zero/1.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c661t-438d23dbf1d0c569c0ac2307f696fb4d4280c76c2070d2937e416798b5b554193</citedby><cites>FETCH-LOGICAL-c661t-438d23dbf1d0c569c0ac2307f696fb4d4280c76c2070d2937e416798b5b554193</cites><orcidid>0000-0003-1328-2695 ; 0000-0003-2338-5698 ; 0000-0001-6320-5597 ; 0000-0001-5229-5750 ; 0000-0001-5010-4586</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7197865/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7197865/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32320442$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gilbert-Girard, Shella</creatorcontrib><creatorcontrib>Gravel, Annie</creatorcontrib><creatorcontrib>Collin, Vanessa</creatorcontrib><creatorcontrib>Wight, Darren J</creatorcontrib><creatorcontrib>Kaufer, Benedikt B</creatorcontrib><creatorcontrib>Lazzerini-Denchi, Eros</creatorcontrib><creatorcontrib>Flamand, Louis</creatorcontrib><title>Role for the shelterin protein TRF2 in human herpesvirus 6A/B chromosomal integration</title><title>PLoS pathogens</title><addtitle>PLoS Pathog</addtitle><description>Human herpesviruses 6A and 6B (HHV-6A/B) are unique among human herpesviruses in their ability to integrate their genome into host chromosomes. Viral integration occurs at the ends of chromosomes within the host telomeres. The ends of the HHV-6A/B genomes contain telomeric repeats that facilitate the integration process. Here, we report that productive infections are associated with a massive increase in telomeric sequences of viral origin. The majority of the viral telomeric signals can be detected within viral replication compartments (VRC) that contain the viral DNA processivity factor p41 and the viral immediate-early 2 (IE2) protein. Components of the shelterin protein complex present at telomeres, including TRF1 and TRF2 are also recruited to VRC during infection. Biochemical, immunofluorescence coupled with in situ hybridization and chromatin immunoprecipitation demonstrated the binding of TRF2 to the HHV-6A/B telomeric repeats. In addition, approximately 60% of the viral IE2 protein localize at cellular telomeres during infection. Transient knockdown of TRF2 resulted in greatly reduced (13%) localization of IE2 at cellular telomeres (p<0.0001). Lastly, TRF2 knockdown reduced HHV-6A/B integration frequency (p<0.05), while no effect was observed on the infection efficiency. Overall, our study identified that HHV-6A/B IE2 localizes to telomeres during infection and highlight the role of TRF2 in HHV-6A/B infection and chromosomal integration.</description><subject>Angina pectoris</subject><subject>Antibodies</subject><subject>Ataxia</subject><subject>Biology and Life Sciences</subject><subject>Cell division</subject><subject>Chromatin</subject><subject>Chromosomes</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA damage</subject><subject>EDTA</subject><subject>Fluorescent antibody technique</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Health aspects</subject><subject>Herpes viruses</subject><subject>Herpesviruses</subject><subject>Human performance</subject><subject>Hybridization</subject><subject>IE2 protein</subject><subject>Immunofluorescence</subject><subject>Immunoprecipitation</subject><subject>Infection</subject><subject>Infections</subject><subject>Infectious 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for the shelterin protein TRF2 in human herpesvirus 6A/B chromosomal integration</title><author>Gilbert-Girard, Shella ; Gravel, Annie ; Collin, Vanessa ; Wight, Darren J ; Kaufer, Benedikt B ; Lazzerini-Denchi, Eros ; Flamand, Louis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c661t-438d23dbf1d0c569c0ac2307f696fb4d4280c76c2070d2937e416798b5b554193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Angina pectoris</topic><topic>Antibodies</topic><topic>Ataxia</topic><topic>Biology and Life Sciences</topic><topic>Cell division</topic><topic>Chromatin</topic><topic>Chromosomes</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA damage</topic><topic>EDTA</topic><topic>Fluorescent antibody technique</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Health aspects</topic><topic>Herpes viruses</topic><topic>Herpesviruses</topic><topic>Human performance</topic><topic>Hybridization</topic><topic>IE2 protein</topic><topic>Immunofluorescence</topic><topic>Immunoprecipitation</topic><topic>Infection</topic><topic>Infections</topic><topic>Infectious diseases</topic><topic>Integration</topic><topic>Localization</topic><topic>Medical research</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Telomerase</topic><topic>Telomere-binding protein</topic><topic>Telomeres</topic><topic>TRF2 protein</topic><topic>Virus replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gilbert-Girard, Shella</creatorcontrib><creatorcontrib>Gravel, Annie</creatorcontrib><creatorcontrib>Collin, Vanessa</creatorcontrib><creatorcontrib>Wight, Darren J</creatorcontrib><creatorcontrib>Kaufer, Benedikt B</creatorcontrib><creatorcontrib>Lazzerini-Denchi, Eros</creatorcontrib><creatorcontrib>Flamand, 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Pathog</addtitle><date>2020-04-01</date><risdate>2020</risdate><volume>16</volume><issue>4</issue><spage>e1008496</spage><epage>e1008496</epage><pages>e1008496-e1008496</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Human herpesviruses 6A and 6B (HHV-6A/B) are unique among human herpesviruses in their ability to integrate their genome into host chromosomes. Viral integration occurs at the ends of chromosomes within the host telomeres. The ends of the HHV-6A/B genomes contain telomeric repeats that facilitate the integration process. Here, we report that productive infections are associated with a massive increase in telomeric sequences of viral origin. The majority of the viral telomeric signals can be detected within viral replication compartments (VRC) that contain the viral DNA processivity factor p41 and the viral immediate-early 2 (IE2) protein. Components of the shelterin protein complex present at telomeres, including TRF1 and TRF2 are also recruited to VRC during infection. Biochemical, immunofluorescence coupled with in situ hybridization and chromatin immunoprecipitation demonstrated the binding of TRF2 to the HHV-6A/B telomeric repeats. In addition, approximately 60% of the viral IE2 protein localize at cellular telomeres during infection. Transient knockdown of TRF2 resulted in greatly reduced (13%) localization of IE2 at cellular telomeres (p<0.0001). Lastly, TRF2 knockdown reduced HHV-6A/B integration frequency (p<0.05), while no effect was observed on the infection efficiency. Overall, our study identified that HHV-6A/B IE2 localizes to telomeres during infection and highlight the role of TRF2 in HHV-6A/B infection and chromosomal integration.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>32320442</pmid><doi>10.1371/journal.ppat.1008496</doi><orcidid>https://orcid.org/0000-0003-1328-2695</orcidid><orcidid>https://orcid.org/0000-0003-2338-5698</orcidid><orcidid>https://orcid.org/0000-0001-6320-5597</orcidid><orcidid>https://orcid.org/0000-0001-5229-5750</orcidid><orcidid>https://orcid.org/0000-0001-5010-4586</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Angina pectoris Antibodies Ataxia Biology and Life Sciences Cell division Chromatin Chromosomes Deoxyribonucleic acid DNA DNA damage EDTA Fluorescent antibody technique Genomes Genomics Health aspects Herpes viruses Herpesviruses Human performance Hybridization IE2 protein Immunofluorescence Immunoprecipitation Infection Infections Infectious diseases Integration Localization Medical research Plasmids Proteins Research and Analysis Methods Telomerase Telomere-binding protein Telomeres TRF2 protein Virus replication |
| title | Role for the shelterin protein TRF2 in human herpesvirus 6A/B chromosomal integration |
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