HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle
N6-methyladenosine (m6A) is the most abundant HIV RNA modification but the interplay between the m6A reader protein YTHDF3 and HIV replication is not well understood. We found that knockout of YTHDF3 in human CD4+ T-cells increases infection supporting the role of YTHDF3 as a restriction factor. Ove...
Gespeichert in:
| Veröffentlicht in: | PLoS pathogens 2020-02, Vol.16 (2), p.e1008305-e1008305 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e1008305 |
|---|---|
| container_issue | 2 |
| container_start_page | e1008305 |
| container_title | PLoS pathogens |
| container_volume | 16 |
| creator | Jurczyszak, Denise Zhang, Wen Terry, Sandra N Kehrer, Thomas Bermúdez González, Maria C McGregor, Emma Mulder, Lubbertus C F Eckwahl, Matthew J Pan, Tao Simon, Viviana |
| description | N6-methyladenosine (m6A) is the most abundant HIV RNA modification but the interplay between the m6A reader protein YTHDF3 and HIV replication is not well understood. We found that knockout of YTHDF3 in human CD4+ T-cells increases infection supporting the role of YTHDF3 as a restriction factor. Overexpression of the YTHDF3 protein in the producer cells reduces the infectivity of the newly produced viruses. YTHDF3 proteins are incorporated into HIV particles in a nucleocapsid-dependent manner permitting the m6A reader protein to limit infection in the new target cell at the step of reverse transcription. Importantly, HIV protease cleaves the virion-incorporated full-length YTHDF3 protein, a process which is blocked by HIV protease inhibitors used to treat HIV infected patients. Mass-spectrometry confirmed the proteolytic processing of YTHDF3 in the virion. Thus, HIV protease cleaves the virion-encapsidated host m6A effector protein in addition to the viral polyproteins to ensure optimal infectivity of the mature virion. |
| doi_str_mv | 10.1371/journal.ppat.1008305 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_plos_</sourceid><recordid>TN_cdi_plos_journals_2377705150</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_0171995c10ab48c9922f508557a02150</doaj_id><sourcerecordid>2355957573</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3715-570079fd48a49694b41d053a2644ce64364289e1ea407156298a25b70e2a18923</originalsourceid><addsrcrecordid>eNptkl9LHDEUxYO0qLV-A9GBvvRltzf_JpOXgtjaXRCEYgWfwt2ZuzrL7GRMZhf67ZvtjKLiUy7J7557bjiMnXCYcmn4t5XfhBabaddhP-UAhQS9xw651nJipFEfXtQH7FOMKwDFJc_32YEUoKUBc8h-z-a3WRd8TxgpKxvCLcWsf6AM277e1gGbbJ2fZ4GwojCQdZvd3cx-XMosVTt0wDoMfZ0UPrOPS2wiHY_nEftz-fPmYja5uv41vzi_mpTJvp5oA2DsslIFKptbtVC8Sq5Q5EqVlCuZK1FY4oQKEp8LW6DQCwMkkBdWyCN2Nuh2jY9u_I7ohDTGgOYaEjEfiMrjynWhXmP46zzW7v-FD_du9OyAG26tLjngQhWltUIsNRRaGwQxaH0fp20Wa6pKavu09CvR1y9t_eDu_dYZUNIUKgl8HQWCf9xQ7N26jiU1DbbkNzvfWltttJEJ_fIGfX87NVBl8DEGWj6b4eB2EXnqcruIuDEiqe305SLPTU-ZkP8AZbi1mg</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2377705150</pqid></control><display><type>article</type><title>HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central Open Access</source><source>Public Library of Science (PLoS) Journals Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Jurczyszak, Denise ; Zhang, Wen ; Terry, Sandra N ; Kehrer, Thomas ; Bermúdez González, Maria C ; McGregor, Emma ; Mulder, Lubbertus C F ; Eckwahl, Matthew J ; Pan, Tao ; Simon, Viviana</creator><contributor>Emerman, Michael</contributor><creatorcontrib>Jurczyszak, Denise ; Zhang, Wen ; Terry, Sandra N ; Kehrer, Thomas ; Bermúdez González, Maria C ; McGregor, Emma ; Mulder, Lubbertus C F ; Eckwahl, Matthew J ; Pan, Tao ; Simon, Viviana ; Emerman, Michael</creatorcontrib><description>N6-methyladenosine (m6A) is the most abundant HIV RNA modification but the interplay between the m6A reader protein YTHDF3 and HIV replication is not well understood. We found that knockout of YTHDF3 in human CD4+ T-cells increases infection supporting the role of YTHDF3 as a restriction factor. Overexpression of the YTHDF3 protein in the producer cells reduces the infectivity of the newly produced viruses. YTHDF3 proteins are incorporated into HIV particles in a nucleocapsid-dependent manner permitting the m6A reader protein to limit infection in the new target cell at the step of reverse transcription. Importantly, HIV protease cleaves the virion-incorporated full-length YTHDF3 protein, a process which is blocked by HIV protease inhibitors used to treat HIV infected patients. Mass-spectrometry confirmed the proteolytic processing of YTHDF3 in the virion. Thus, HIV protease cleaves the virion-encapsidated host m6A effector protein in addition to the viral polyproteins to ensure optimal infectivity of the mature virion.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1008305</identifier><identifier>PMID: 32053707</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adenosine - analogs & derivatives ; Adenosine - genetics ; Adenosine - metabolism ; Antiviral Agents - metabolism ; Biochemistry ; Biology and Life Sciences ; CD4 antigen ; CD4-Positive T-Lymphocytes - metabolism ; CD4-Positive T-Lymphocytes - virology ; CRISPR ; Experiments ; Funding ; HEK293 Cells ; HIV ; HIV Infections - virology ; HIV Protease - metabolism ; HIV Protease - physiology ; HIV-1 - genetics ; Human immunodeficiency virus ; Humans ; Infections ; Infectivity ; Lymphocytes ; Lymphocytes T ; Medicine ; Medicine and Health Sciences ; Molecular biology ; N6-methyladenosine ; Nucleocapsids ; Pathogens ; Polyproteins ; Primary Cell Culture ; Producer cells ; Protease ; Protease inhibitors ; Proteinase inhibitors ; Proteins ; Proteolysis ; Research and analysis methods ; Reverse transcription ; RNA modification ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Spectrometry ; Supervision ; Virion - metabolism ; Virions ; Viruses ; West Nile virus</subject><ispartof>PLoS pathogens, 2020-02, Vol.16 (2), p.e1008305-e1008305</ispartof><rights>2020 Jurczyszak et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 Jurczyszak et al 2020 Jurczyszak et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3715-570079fd48a49694b41d053a2644ce64364289e1ea407156298a25b70e2a18923</citedby><cites>FETCH-LOGICAL-c3715-570079fd48a49694b41d053a2644ce64364289e1ea407156298a25b70e2a18923</cites><orcidid>0000-0003-4634-5672 ; 0000-0002-6416-5096 ; 0000-0001-8577-2613 ; 0000-0002-3625-4016 ; 0000-0003-1096-8405 ; 0000-0002-6433-0098</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/PMC7043784/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7043784/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32053707$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Emerman, Michael</contributor><creatorcontrib>Jurczyszak, Denise</creatorcontrib><creatorcontrib>Zhang, Wen</creatorcontrib><creatorcontrib>Terry, Sandra N</creatorcontrib><creatorcontrib>Kehrer, Thomas</creatorcontrib><creatorcontrib>Bermúdez González, Maria C</creatorcontrib><creatorcontrib>McGregor, Emma</creatorcontrib><creatorcontrib>Mulder, Lubbertus C F</creatorcontrib><creatorcontrib>Eckwahl, Matthew J</creatorcontrib><creatorcontrib>Pan, Tao</creatorcontrib><creatorcontrib>Simon, Viviana</creatorcontrib><title>HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle</title><title>PLoS pathogens</title><addtitle>PLoS Pathog</addtitle><description>N6-methyladenosine (m6A) is the most abundant HIV RNA modification but the interplay between the m6A reader protein YTHDF3 and HIV replication is not well understood. We found that knockout of YTHDF3 in human CD4+ T-cells increases infection supporting the role of YTHDF3 as a restriction factor. Overexpression of the YTHDF3 protein in the producer cells reduces the infectivity of the newly produced viruses. YTHDF3 proteins are incorporated into HIV particles in a nucleocapsid-dependent manner permitting the m6A reader protein to limit infection in the new target cell at the step of reverse transcription. Importantly, HIV protease cleaves the virion-incorporated full-length YTHDF3 protein, a process which is blocked by HIV protease inhibitors used to treat HIV infected patients. Mass-spectrometry confirmed the proteolytic processing of YTHDF3 in the virion. Thus, HIV protease cleaves the virion-encapsidated host m6A effector protein in addition to the viral polyproteins to ensure optimal infectivity of the mature virion.</description><subject>Adenosine - analogs & derivatives</subject><subject>Adenosine - genetics</subject><subject>Adenosine - metabolism</subject><subject>Antiviral Agents - metabolism</subject><subject>Biochemistry</subject><subject>Biology and Life Sciences</subject><subject>CD4 antigen</subject><subject>CD4-Positive T-Lymphocytes - metabolism</subject><subject>CD4-Positive T-Lymphocytes - virology</subject><subject>CRISPR</subject><subject>Experiments</subject><subject>Funding</subject><subject>HEK293 Cells</subject><subject>HIV</subject><subject>HIV Infections - virology</subject><subject>HIV Protease - metabolism</subject><subject>HIV Protease - physiology</subject><subject>HIV-1 - genetics</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Infections</subject><subject>Infectivity</subject><subject>Lymphocytes</subject><subject>Lymphocytes T</subject><subject>Medicine</subject><subject>Medicine and Health Sciences</subject><subject>Molecular biology</subject><subject>N6-methyladenosine</subject><subject>Nucleocapsids</subject><subject>Pathogens</subject><subject>Polyproteins</subject><subject>Primary Cell Culture</subject><subject>Producer cells</subject><subject>Protease</subject><subject>Protease inhibitors</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Research and analysis methods</subject><subject>Reverse transcription</subject><subject>RNA modification</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Spectrometry</subject><subject>Supervision</subject><subject>Virion - metabolism</subject><subject>Virions</subject><subject>Viruses</subject><subject>West Nile virus</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNptkl9LHDEUxYO0qLV-A9GBvvRltzf_JpOXgtjaXRCEYgWfwt2ZuzrL7GRMZhf67ZvtjKLiUy7J7557bjiMnXCYcmn4t5XfhBabaddhP-UAhQS9xw651nJipFEfXtQH7FOMKwDFJc_32YEUoKUBc8h-z-a3WRd8TxgpKxvCLcWsf6AM277e1gGbbJ2fZ4GwojCQdZvd3cx-XMosVTt0wDoMfZ0UPrOPS2wiHY_nEftz-fPmYja5uv41vzi_mpTJvp5oA2DsslIFKptbtVC8Sq5Q5EqVlCuZK1FY4oQKEp8LW6DQCwMkkBdWyCN2Nuh2jY9u_I7ohDTGgOYaEjEfiMrjynWhXmP46zzW7v-FD_du9OyAG26tLjngQhWltUIsNRRaGwQxaH0fp20Wa6pKavu09CvR1y9t_eDu_dYZUNIUKgl8HQWCf9xQ7N26jiU1DbbkNzvfWltttJEJ_fIGfX87NVBl8DEGWj6b4eB2EXnqcruIuDEiqe305SLPTU-ZkP8AZbi1mg</recordid><startdate>202002</startdate><enddate>202002</enddate><creator>Jurczyszak, Denise</creator><creator>Zhang, Wen</creator><creator>Terry, Sandra N</creator><creator>Kehrer, Thomas</creator><creator>Bermúdez González, Maria C</creator><creator>McGregor, Emma</creator><creator>Mulder, Lubbertus C F</creator><creator>Eckwahl, Matthew J</creator><creator>Pan, Tao</creator><creator>Simon, Viviana</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-4634-5672</orcidid><orcidid>https://orcid.org/0000-0002-6416-5096</orcidid><orcidid>https://orcid.org/0000-0001-8577-2613</orcidid><orcidid>https://orcid.org/0000-0002-3625-4016</orcidid><orcidid>https://orcid.org/0000-0003-1096-8405</orcidid><orcidid>https://orcid.org/0000-0002-6433-0098</orcidid></search><sort><creationdate>202002</creationdate><title>HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle</title><author>Jurczyszak, Denise ; Zhang, Wen ; Terry, Sandra N ; Kehrer, Thomas ; Bermúdez González, Maria C ; McGregor, Emma ; Mulder, Lubbertus C F ; Eckwahl, Matthew J ; Pan, Tao ; Simon, Viviana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3715-570079fd48a49694b41d053a2644ce64364289e1ea407156298a25b70e2a18923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adenosine - analogs & derivatives</topic><topic>Adenosine - genetics</topic><topic>Adenosine - metabolism</topic><topic>Antiviral Agents - metabolism</topic><topic>Biochemistry</topic><topic>Biology and Life Sciences</topic><topic>CD4 antigen</topic><topic>CD4-Positive T-Lymphocytes - metabolism</topic><topic>CD4-Positive T-Lymphocytes - virology</topic><topic>CRISPR</topic><topic>Experiments</topic><topic>Funding</topic><topic>HEK293 Cells</topic><topic>HIV</topic><topic>HIV Infections - virology</topic><topic>HIV Protease - metabolism</topic><topic>HIV Protease - physiology</topic><topic>HIV-1 - genetics</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Infections</topic><topic>Infectivity</topic><topic>Lymphocytes</topic><topic>Lymphocytes T</topic><topic>Medicine</topic><topic>Medicine and Health Sciences</topic><topic>Molecular biology</topic><topic>N6-methyladenosine</topic><topic>Nucleocapsids</topic><topic>Pathogens</topic><topic>Polyproteins</topic><topic>Primary Cell Culture</topic><topic>Producer cells</topic><topic>Protease</topic><topic>Protease inhibitors</topic><topic>Proteinase inhibitors</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Research and analysis methods</topic><topic>Reverse transcription</topic><topic>RNA modification</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Spectrometry</topic><topic>Supervision</topic><topic>Virion - metabolism</topic><topic>Virions</topic><topic>Viruses</topic><topic>West Nile virus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jurczyszak, Denise</creatorcontrib><creatorcontrib>Zhang, Wen</creatorcontrib><creatorcontrib>Terry, Sandra N</creatorcontrib><creatorcontrib>Kehrer, Thomas</creatorcontrib><creatorcontrib>Bermúdez González, Maria C</creatorcontrib><creatorcontrib>McGregor, Emma</creatorcontrib><creatorcontrib>Mulder, Lubbertus C F</creatorcontrib><creatorcontrib>Eckwahl, Matthew J</creatorcontrib><creatorcontrib>Pan, Tao</creatorcontrib><creatorcontrib>Simon, Viviana</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jurczyszak, Denise</au><au>Zhang, Wen</au><au>Terry, Sandra N</au><au>Kehrer, Thomas</au><au>Bermúdez González, Maria C</au><au>McGregor, Emma</au><au>Mulder, Lubbertus C F</au><au>Eckwahl, Matthew J</au><au>Pan, Tao</au><au>Simon, Viviana</au><au>Emerman, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2020-02</date><risdate>2020</risdate><volume>16</volume><issue>2</issue><spage>e1008305</spage><epage>e1008305</epage><pages>e1008305-e1008305</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>N6-methyladenosine (m6A) is the most abundant HIV RNA modification but the interplay between the m6A reader protein YTHDF3 and HIV replication is not well understood. We found that knockout of YTHDF3 in human CD4+ T-cells increases infection supporting the role of YTHDF3 as a restriction factor. Overexpression of the YTHDF3 protein in the producer cells reduces the infectivity of the newly produced viruses. YTHDF3 proteins are incorporated into HIV particles in a nucleocapsid-dependent manner permitting the m6A reader protein to limit infection in the new target cell at the step of reverse transcription. Importantly, HIV protease cleaves the virion-incorporated full-length YTHDF3 protein, a process which is blocked by HIV protease inhibitors used to treat HIV infected patients. Mass-spectrometry confirmed the proteolytic processing of YTHDF3 in the virion. Thus, HIV protease cleaves the virion-encapsidated host m6A effector protein in addition to the viral polyproteins to ensure optimal infectivity of the mature virion.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>32053707</pmid><doi>10.1371/journal.ppat.1008305</doi><orcidid>https://orcid.org/0000-0003-4634-5672</orcidid><orcidid>https://orcid.org/0000-0002-6416-5096</orcidid><orcidid>https://orcid.org/0000-0001-8577-2613</orcidid><orcidid>https://orcid.org/0000-0002-3625-4016</orcidid><orcidid>https://orcid.org/0000-0003-1096-8405</orcidid><orcidid>https://orcid.org/0000-0002-6433-0098</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1553-7374 |
| ispartof | PLoS pathogens, 2020-02, Vol.16 (2), p.e1008305-e1008305 |
| issn | 1553-7374 1553-7366 1553-7374 |
| language | eng |
| recordid | cdi_plos_journals_2377705150 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; PubMed Central Open Access; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adenosine - analogs & derivatives Adenosine - genetics Adenosine - metabolism Antiviral Agents - metabolism Biochemistry Biology and Life Sciences CD4 antigen CD4-Positive T-Lymphocytes - metabolism CD4-Positive T-Lymphocytes - virology CRISPR Experiments Funding HEK293 Cells HIV HIV Infections - virology HIV Protease - metabolism HIV Protease - physiology HIV-1 - genetics Human immunodeficiency virus Humans Infections Infectivity Lymphocytes Lymphocytes T Medicine Medicine and Health Sciences Molecular biology N6-methyladenosine Nucleocapsids Pathogens Polyproteins Primary Cell Culture Producer cells Protease Protease inhibitors Proteinase inhibitors Proteins Proteolysis Research and analysis methods Reverse transcription RNA modification RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Spectrometry Supervision Virion - metabolism Virions Viruses West Nile virus |
| title | HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T14%3A52%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=HIV%20protease%20cleaves%20the%20antiviral%20m6A%20reader%20protein%20YTHDF3%20in%20the%20viral%20particle&rft.jtitle=PLoS%20pathogens&rft.au=Jurczyszak,%20Denise&rft.date=2020-02&rft.volume=16&rft.issue=2&rft.spage=e1008305&rft.epage=e1008305&rft.pages=e1008305-e1008305&rft.issn=1553-7374&rft.eissn=1553-7374&rft_id=info:doi/10.1371/journal.ppat.1008305&rft_dat=%3Cproquest_plos_%3E2355957573%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2377705150&rft_id=info:pmid/32053707&rft_doaj_id=oai_doaj_org_article_0171995c10ab48c9922f508557a02150&rfr_iscdi=true |