Loading…
IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis
The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP , transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate...
Saved in:
| Published in: | eLife 2018-05, Vol.7 |
|---|---|
| Main Authors: | , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23 |
| container_end_page | |
| container_issue | |
| container_start_page | |
| container_title | eLife |
| container_volume | 7 |
| creator | Mallery, Donna L Márquez, Chantal L McEwan, William A Dickson, Claire F Jacques, David A Anandapadamanaban, Madhanagopal Bichel, Katsiaryna Towers, Gregory J Saiardi, Adolfo Böcking, Till James, Leo C |
| description | The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP
, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP
, which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP
, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP
molecules per infectious virion. We propose that HIV recruits IP
to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP
/capsid/co-factor/reverse transcription. |
| doi_str_mv | 10.7554/eLife.35335 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_7c6859948eca463995437484988a1476</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_7c6859948eca463995437484988a1476</doaj_id><sourcerecordid>2080668822</sourcerecordid><originalsourceid>FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23</originalsourceid><addsrcrecordid>eNpVkcFPHCEUxknTphr11HtD4rFZhQGGx8XEaFs32dgebNMbYZg37qyzwwisif99cVeNcuGF9_Hje3yEfOHsRCslT3HRd3gilBDqA9mvmGIzBvLfxzf1HjlKacXK0hKAm89krzIgQUq-T27mv2vaJ-pGejX_S6fg7zDTzvkcIs1Ll-kU8QHHnKh3U-pb6sMwlArLlbY0wzpkTPTy-pymxzEvMfXpkHzq3JDw6Hk_IH9-fL-5uJotfv2cX5wvZl5xnWeOtxqc6IpTdAIUb1SnuEHjVeV1w2qopBYNKO00dshQOMm55g3KBrqmEgdkvuO2wa3sFPu1i482uN5uD0K8tS7m3g9ota9BGSMBvZO1MEZJUb5DGgDHpa4L62zHmjbNGltfRo5ueAd93xn7pb0ND7ZmwnANBXD8DIjhfoMp21XYxLHMbysGrK4BqifL33YqH0NKEbvXFzizT4nabaJ2m2hRf31r6lX7kp_4D6UMmw0</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2080668822</pqid></control><display><type>article</type><title>IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis</title><source>PubMed Central Free</source><source>Publicly Available Content Database</source><creator>Mallery, Donna L ; Márquez, Chantal L ; McEwan, William A ; Dickson, Claire F ; Jacques, David A ; Anandapadamanaban, Madhanagopal ; Bichel, Katsiaryna ; Towers, Gregory J ; Saiardi, Adolfo ; Böcking, Till ; James, Leo C</creator><creatorcontrib>Mallery, Donna L ; Márquez, Chantal L ; McEwan, William A ; Dickson, Claire F ; Jacques, David A ; Anandapadamanaban, Madhanagopal ; Bichel, Katsiaryna ; Towers, Gregory J ; Saiardi, Adolfo ; Böcking, Till ; James, Leo C</creatorcontrib><description>The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP
, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP
, which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP
, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP
molecules per infectious virion. We propose that HIV recruits IP
to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP
/capsid/co-factor/reverse transcription.</description><identifier>ISSN: 2050-084X</identifier><identifier>EISSN: 2050-084X</identifier><identifier>DOI: 10.7554/eLife.35335</identifier><identifier>PMID: 29848441</identifier><language>eng</language><publisher>England: eLife Sciences Publications Ltd</publisher><subject>Adenosine Triphosphate - metabolism ; Arginine ; Biology ; capsid ; Capsid - metabolism ; Capsid - ultrastructure ; Capsids ; Data collection ; Deoxyribonucleic acid ; DNA ; DNA biosynthesis ; DNA, Viral - biosynthesis ; HEK293 Cells ; Hexamers ; HIV ; HIV-1 - metabolism ; HIV-1 - ultrastructure ; Human immunodeficiency virus ; Humans ; Infections ; Inositol ; IP6 ; Labeling ; Laboratories ; Medical research ; Microbiology and Infectious Disease ; Nucleotides - metabolism ; Polyelectrolytes ; Polymers - metabolism ; Pores ; Reverse Transcriptase Inhibitors - pharmacology ; Reverse transcription ; Reverse Transcription - drug effects ; Reverse Transcription - genetics ; Structural Biology and Molecular Biophysics ; Subtilisin - metabolism ; Uncoating ; University colleges ; Virion - drug effects ; Virion - metabolism ; Virions ; Virus Assembly - drug effects</subject><ispartof>eLife, 2018-05, Vol.7</ispartof><rights>2018, Mallery et al.</rights><rights>2018, Mallery et al. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2018, Mallery et al 2018 Mallery et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23</citedby><cites>FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23</cites><orcidid>0000-0002-4408-0407 ; 0000-0002-6426-4510 ; 0000-0003-2131-0334 ; 0000-0003-1165-3122</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2080668822/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2080668822?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29848441$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mallery, Donna L</creatorcontrib><creatorcontrib>Márquez, Chantal L</creatorcontrib><creatorcontrib>McEwan, William A</creatorcontrib><creatorcontrib>Dickson, Claire F</creatorcontrib><creatorcontrib>Jacques, David A</creatorcontrib><creatorcontrib>Anandapadamanaban, Madhanagopal</creatorcontrib><creatorcontrib>Bichel, Katsiaryna</creatorcontrib><creatorcontrib>Towers, Gregory J</creatorcontrib><creatorcontrib>Saiardi, Adolfo</creatorcontrib><creatorcontrib>Böcking, Till</creatorcontrib><creatorcontrib>James, Leo C</creatorcontrib><title>IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis</title><title>eLife</title><addtitle>Elife</addtitle><description>The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP
, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP
, which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP
, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP
molecules per infectious virion. We propose that HIV recruits IP
to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP
/capsid/co-factor/reverse transcription.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Arginine</subject><subject>Biology</subject><subject>capsid</subject><subject>Capsid - metabolism</subject><subject>Capsid - ultrastructure</subject><subject>Capsids</subject><subject>Data collection</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA biosynthesis</subject><subject>DNA, Viral - biosynthesis</subject><subject>HEK293 Cells</subject><subject>Hexamers</subject><subject>HIV</subject><subject>HIV-1 - metabolism</subject><subject>HIV-1 - ultrastructure</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Infections</subject><subject>Inositol</subject><subject>IP6</subject><subject>Labeling</subject><subject>Laboratories</subject><subject>Medical research</subject><subject>Microbiology and Infectious Disease</subject><subject>Nucleotides - metabolism</subject><subject>Polyelectrolytes</subject><subject>Polymers - metabolism</subject><subject>Pores</subject><subject>Reverse Transcriptase Inhibitors - pharmacology</subject><subject>Reverse transcription</subject><subject>Reverse Transcription - drug effects</subject><subject>Reverse Transcription - genetics</subject><subject>Structural Biology and Molecular Biophysics</subject><subject>Subtilisin - metabolism</subject><subject>Uncoating</subject><subject>University colleges</subject><subject>Virion - drug effects</subject><subject>Virion - metabolism</subject><subject>Virions</subject><subject>Virus Assembly - drug effects</subject><issn>2050-084X</issn><issn>2050-084X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpVkcFPHCEUxknTphr11HtD4rFZhQGGx8XEaFs32dgebNMbYZg37qyzwwisif99cVeNcuGF9_Hje3yEfOHsRCslT3HRd3gilBDqA9mvmGIzBvLfxzf1HjlKacXK0hKAm89krzIgQUq-T27mv2vaJ-pGejX_S6fg7zDTzvkcIs1Ll-kU8QHHnKh3U-pb6sMwlArLlbY0wzpkTPTy-pymxzEvMfXpkHzq3JDw6Hk_IH9-fL-5uJotfv2cX5wvZl5xnWeOtxqc6IpTdAIUb1SnuEHjVeV1w2qopBYNKO00dshQOMm55g3KBrqmEgdkvuO2wa3sFPu1i482uN5uD0K8tS7m3g9ota9BGSMBvZO1MEZJUb5DGgDHpa4L62zHmjbNGltfRo5ueAd93xn7pb0ND7ZmwnANBXD8DIjhfoMp21XYxLHMbysGrK4BqifL33YqH0NKEbvXFzizT4nabaJ2m2hRf31r6lX7kp_4D6UMmw0</recordid><startdate>20180531</startdate><enddate>20180531</enddate><creator>Mallery, Donna L</creator><creator>Márquez, Chantal L</creator><creator>McEwan, William A</creator><creator>Dickson, Claire F</creator><creator>Jacques, David A</creator><creator>Anandapadamanaban, Madhanagopal</creator><creator>Bichel, Katsiaryna</creator><creator>Towers, Gregory J</creator><creator>Saiardi, Adolfo</creator><creator>Böcking, Till</creator><creator>James, Leo C</creator><general>eLife Sciences Publications Ltd</general><general>eLife Sciences Publications, Ltd</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>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</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>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-4408-0407</orcidid><orcidid>https://orcid.org/0000-0002-6426-4510</orcidid><orcidid>https://orcid.org/0000-0003-2131-0334</orcidid><orcidid>https://orcid.org/0000-0003-1165-3122</orcidid></search><sort><creationdate>20180531</creationdate><title>IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis</title><author>Mallery, Donna L ; Márquez, Chantal L ; McEwan, William A ; Dickson, Claire F ; Jacques, David A ; Anandapadamanaban, Madhanagopal ; Bichel, Katsiaryna ; Towers, Gregory J ; Saiardi, Adolfo ; Böcking, Till ; James, Leo C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Arginine</topic><topic>Biology</topic><topic>capsid</topic><topic>Capsid - metabolism</topic><topic>Capsid - ultrastructure</topic><topic>Capsids</topic><topic>Data collection</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA biosynthesis</topic><topic>DNA, Viral - biosynthesis</topic><topic>HEK293 Cells</topic><topic>Hexamers</topic><topic>HIV</topic><topic>HIV-1 - metabolism</topic><topic>HIV-1 - ultrastructure</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Infections</topic><topic>Inositol</topic><topic>IP6</topic><topic>Labeling</topic><topic>Laboratories</topic><topic>Medical research</topic><topic>Microbiology and Infectious Disease</topic><topic>Nucleotides - metabolism</topic><topic>Polyelectrolytes</topic><topic>Polymers - metabolism</topic><topic>Pores</topic><topic>Reverse Transcriptase Inhibitors - pharmacology</topic><topic>Reverse transcription</topic><topic>Reverse Transcription - drug effects</topic><topic>Reverse Transcription - genetics</topic><topic>Structural Biology and Molecular Biophysics</topic><topic>Subtilisin - metabolism</topic><topic>Uncoating</topic><topic>University colleges</topic><topic>Virion - drug effects</topic><topic>Virion - metabolism</topic><topic>Virions</topic><topic>Virus Assembly - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mallery, Donna L</creatorcontrib><creatorcontrib>Márquez, Chantal L</creatorcontrib><creatorcontrib>McEwan, William A</creatorcontrib><creatorcontrib>Dickson, Claire F</creatorcontrib><creatorcontrib>Jacques, David A</creatorcontrib><creatorcontrib>Anandapadamanaban, Madhanagopal</creatorcontrib><creatorcontrib>Bichel, Katsiaryna</creatorcontrib><creatorcontrib>Towers, Gregory J</creatorcontrib><creatorcontrib>Saiardi, Adolfo</creatorcontrib><creatorcontrib>Böcking, Till</creatorcontrib><creatorcontrib>James, Leo C</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>Health & Medical Collection (ProQuest Medical & Health Databases)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science 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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</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>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>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>ProQuest Biological Science Journals</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>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>eLife</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mallery, Donna L</au><au>Márquez, Chantal L</au><au>McEwan, William A</au><au>Dickson, Claire F</au><au>Jacques, David A</au><au>Anandapadamanaban, Madhanagopal</au><au>Bichel, Katsiaryna</au><au>Towers, Gregory J</au><au>Saiardi, Adolfo</au><au>Böcking, Till</au><au>James, Leo C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis</atitle><jtitle>eLife</jtitle><addtitle>Elife</addtitle><date>2018-05-31</date><risdate>2018</risdate><volume>7</volume><issn>2050-084X</issn><eissn>2050-084X</eissn><abstract>The HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP
, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP
, which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP
, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP
molecules per infectious virion. We propose that HIV recruits IP
to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP
/capsid/co-factor/reverse transcription.</abstract><cop>England</cop><pub>eLife Sciences Publications Ltd</pub><pmid>29848441</pmid><doi>10.7554/eLife.35335</doi><orcidid>https://orcid.org/0000-0002-4408-0407</orcidid><orcidid>https://orcid.org/0000-0002-6426-4510</orcidid><orcidid>https://orcid.org/0000-0003-2131-0334</orcidid><orcidid>https://orcid.org/0000-0003-1165-3122</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2050-084X |
| ispartof | eLife, 2018-05, Vol.7 |
| issn | 2050-084X 2050-084X |
| language | eng |
| recordid | cdi_doaj_primary_oai_doaj_org_article_7c6859948eca463995437484988a1476 |
| source | PubMed Central Free; Publicly Available Content Database |
| subjects | Adenosine Triphosphate - metabolism Arginine Biology capsid Capsid - metabolism Capsid - ultrastructure Capsids Data collection Deoxyribonucleic acid DNA DNA biosynthesis DNA, Viral - biosynthesis HEK293 Cells Hexamers HIV HIV-1 - metabolism HIV-1 - ultrastructure Human immunodeficiency virus Humans Infections Inositol IP6 Labeling Laboratories Medical research Microbiology and Infectious Disease Nucleotides - metabolism Polyelectrolytes Polymers - metabolism Pores Reverse Transcriptase Inhibitors - pharmacology Reverse transcription Reverse Transcription - drug effects Reverse Transcription - genetics Structural Biology and Molecular Biophysics Subtilisin - metabolism Uncoating University colleges Virion - drug effects Virion - metabolism Virions Virus Assembly - drug effects |
| title | IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T12%3A49%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=IP6%20is%20an%20HIV%20pocket%20factor%20that%20prevents%20capsid%20collapse%20and%20promotes%20DNA%20synthesis&rft.jtitle=eLife&rft.au=Mallery,%20Donna%20L&rft.date=2018-05-31&rft.volume=7&rft.issn=2050-084X&rft.eissn=2050-084X&rft_id=info:doi/10.7554/eLife.35335&rft_dat=%3Cproquest_doaj_%3E2080668822%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c517t-a1d78a3f205ea3851b5f519e9c52c7b0682473b857a7efe0e3a41171be4b8fb23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2080668822&rft_id=info:pmid/29848441&rfr_iscdi=true |