Identification of drug resistance mutations in HIV from constraints on natural evolution

Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape. Here we show that an Ising model describing these interactions, inferred from sequence data obtained prior to the use of antiretro...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Physical review. E 2016-02, Vol.93 (2), p.022412-022412, Article 022412
Hauptverfasser: Butler, Thomas C, Barton, John P, Kardar, Mehran, Chakraborty, Arup K
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 022412
container_issue 2
container_start_page 022412
container_title Physical review. E
container_volume 93
creator Butler, Thomas C
Barton, John P
Kardar, Mehran
Chakraborty, Arup K
description Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape. Here we show that an Ising model describing these interactions, inferred from sequence data obtained prior to the use of antiretroviral drugs, can be used to identify clinically significant sites of resistance mutations. Successful predictions of the resistance sites indicate progress in the development of successful models of real viral evolution at the single residue level and suggest that our approach may be applied to help design new therapies that are less prone to failure even where resistance data are not yet available.
doi_str_mv 10.1103/PhysRevE.93.022412
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1805483285</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1805483285</sourcerecordid><originalsourceid>FETCH-LOGICAL-c413t-e94cb8855b0aa0f439dd06bd0a9d460b217e91f24c1078dd7c29cddc82155453</originalsourceid><addsrcrecordid>eNo9kE1LAzEQhoMottT-AQ-So5fWydfu5iil2kJBkSLeQjbJamQ_apIt9N_b2trTDDPP-x4ehG4JTAkB9vD6tYtvbjufSjYFSjmhF2hIeQ4TAMEuzzsXAzSO8RsASAYyJ_QaDWgmi4xl-RB9LK1rk6-80cl3Le4qbEP_iYOLPibdGoebPv39IvYtXizfcRW6Bpv9IQXt2xTxPtfq1AddY7ft6v5A36CrStfRjU9zhNZP8_VsMVm9PC9nj6uJ4YSliZPclEUhRAlaQ8WZtBay0oKWlmdQUpI7SSrKDYG8sDY3VBprTUGJEFywEbo_1m5C99O7mFTjo3F1rVvX9VGRAgQvGC0OKD2iJnQxBlepTfCNDjtFQB2cqn-nSjJ1dLoP3Z36-7Jx9hz5N8h-AUggdNk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1805483285</pqid></control><display><type>article</type><title>Identification of drug resistance mutations in HIV from constraints on natural evolution</title><source>MEDLINE</source><source>American Physical Society Journals</source><creator>Butler, Thomas C ; Barton, John P ; Kardar, Mehran ; Chakraborty, Arup K</creator><creatorcontrib>Butler, Thomas C ; Barton, John P ; Kardar, Mehran ; Chakraborty, Arup K</creatorcontrib><description>Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape. Here we show that an Ising model describing these interactions, inferred from sequence data obtained prior to the use of antiretroviral drugs, can be used to identify clinically significant sites of resistance mutations. Successful predictions of the resistance sites indicate progress in the development of successful models of real viral evolution at the single residue level and suggest that our approach may be applied to help design new therapies that are less prone to failure even where resistance data are not yet available.</description><identifier>ISSN: 2470-0045</identifier><identifier>EISSN: 2470-0053</identifier><identifier>DOI: 10.1103/PhysRevE.93.022412</identifier><identifier>PMID: 26986367</identifier><language>eng</language><publisher>United States</publisher><subject>Drug Interactions ; Drug Resistance, Viral - genetics ; Evolution, Molecular ; HIV - drug effects ; HIV - enzymology ; HIV - genetics ; HIV Protease - genetics ; HIV Protease Inhibitors - pharmacology ; Humans ; Mutation</subject><ispartof>Physical review. E, 2016-02, Vol.93 (2), p.022412-022412, Article 022412</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-e94cb8855b0aa0f439dd06bd0a9d460b217e91f24c1078dd7c29cddc82155453</citedby><cites>FETCH-LOGICAL-c413t-e94cb8855b0aa0f439dd06bd0a9d460b217e91f24c1078dd7c29cddc82155453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,2863,2864,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26986367$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Butler, Thomas C</creatorcontrib><creatorcontrib>Barton, John P</creatorcontrib><creatorcontrib>Kardar, Mehran</creatorcontrib><creatorcontrib>Chakraborty, Arup K</creatorcontrib><title>Identification of drug resistance mutations in HIV from constraints on natural evolution</title><title>Physical review. E</title><addtitle>Phys Rev E</addtitle><description>Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape. Here we show that an Ising model describing these interactions, inferred from sequence data obtained prior to the use of antiretroviral drugs, can be used to identify clinically significant sites of resistance mutations. Successful predictions of the resistance sites indicate progress in the development of successful models of real viral evolution at the single residue level and suggest that our approach may be applied to help design new therapies that are less prone to failure even where resistance data are not yet available.</description><subject>Drug Interactions</subject><subject>Drug Resistance, Viral - genetics</subject><subject>Evolution, Molecular</subject><subject>HIV - drug effects</subject><subject>HIV - enzymology</subject><subject>HIV - genetics</subject><subject>HIV Protease - genetics</subject><subject>HIV Protease Inhibitors - pharmacology</subject><subject>Humans</subject><subject>Mutation</subject><issn>2470-0045</issn><issn>2470-0053</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LAzEQhoMottT-AQ-So5fWydfu5iil2kJBkSLeQjbJamQ_apIt9N_b2trTDDPP-x4ehG4JTAkB9vD6tYtvbjufSjYFSjmhF2hIeQ4TAMEuzzsXAzSO8RsASAYyJ_QaDWgmi4xl-RB9LK1rk6-80cl3Le4qbEP_iYOLPibdGoebPv39IvYtXizfcRW6Bpv9IQXt2xTxPtfq1AddY7ft6v5A36CrStfRjU9zhNZP8_VsMVm9PC9nj6uJ4YSliZPclEUhRAlaQ8WZtBay0oKWlmdQUpI7SSrKDYG8sDY3VBprTUGJEFywEbo_1m5C99O7mFTjo3F1rVvX9VGRAgQvGC0OKD2iJnQxBlepTfCNDjtFQB2cqn-nSjJ1dLoP3Z36-7Jx9hz5N8h-AUggdNk</recordid><startdate>20160219</startdate><enddate>20160219</enddate><creator>Butler, Thomas C</creator><creator>Barton, John P</creator><creator>Kardar, Mehran</creator><creator>Chakraborty, Arup K</creator><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></search><sort><creationdate>20160219</creationdate><title>Identification of drug resistance mutations in HIV from constraints on natural evolution</title><author>Butler, Thomas C ; Barton, John P ; Kardar, Mehran ; Chakraborty, Arup K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-e94cb8855b0aa0f439dd06bd0a9d460b217e91f24c1078dd7c29cddc82155453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Drug Interactions</topic><topic>Drug Resistance, Viral - genetics</topic><topic>Evolution, Molecular</topic><topic>HIV - drug effects</topic><topic>HIV - enzymology</topic><topic>HIV - genetics</topic><topic>HIV Protease - genetics</topic><topic>HIV Protease Inhibitors - pharmacology</topic><topic>Humans</topic><topic>Mutation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Butler, Thomas C</creatorcontrib><creatorcontrib>Barton, John P</creatorcontrib><creatorcontrib>Kardar, Mehran</creatorcontrib><creatorcontrib>Chakraborty, Arup K</creatorcontrib><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><jtitle>Physical review. E</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Butler, Thomas C</au><au>Barton, John P</au><au>Kardar, Mehran</au><au>Chakraborty, Arup K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of drug resistance mutations in HIV from constraints on natural evolution</atitle><jtitle>Physical review. E</jtitle><addtitle>Phys Rev E</addtitle><date>2016-02-19</date><risdate>2016</risdate><volume>93</volume><issue>2</issue><spage>022412</spage><epage>022412</epage><pages>022412-022412</pages><artnum>022412</artnum><issn>2470-0045</issn><eissn>2470-0053</eissn><abstract>Human immunodeficiency virus (HIV) evolves with extraordinary rapidity. However, its evolution is constrained by interactions between mutations in its fitness landscape. Here we show that an Ising model describing these interactions, inferred from sequence data obtained prior to the use of antiretroviral drugs, can be used to identify clinically significant sites of resistance mutations. Successful predictions of the resistance sites indicate progress in the development of successful models of real viral evolution at the single residue level and suggest that our approach may be applied to help design new therapies that are less prone to failure even where resistance data are not yet available.</abstract><cop>United States</cop><pmid>26986367</pmid><doi>10.1103/PhysRevE.93.022412</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2470-0045
ispartof Physical review. E, 2016-02, Vol.93 (2), p.022412-022412, Article 022412
issn 2470-0045
2470-0053
language eng
recordid cdi_proquest_miscellaneous_1805483285
source MEDLINE; American Physical Society Journals
subjects Drug Interactions
Drug Resistance, Viral - genetics
Evolution, Molecular
HIV - drug effects
HIV - enzymology
HIV - genetics
HIV Protease - genetics
HIV Protease Inhibitors - pharmacology
Humans
Mutation
title Identification of drug resistance mutations in HIV from constraints on natural evolution
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T00%3A15%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20drug%20resistance%20mutations%20in%20HIV%20from%20constraints%20on%20natural%20evolution&rft.jtitle=Physical%20review.%20E&rft.au=Butler,%20Thomas%20C&rft.date=2016-02-19&rft.volume=93&rft.issue=2&rft.spage=022412&rft.epage=022412&rft.pages=022412-022412&rft.artnum=022412&rft.issn=2470-0045&rft.eissn=2470-0053&rft_id=info:doi/10.1103/PhysRevE.93.022412&rft_dat=%3Cproquest_cross%3E1805483285%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1805483285&rft_id=info:pmid/26986367&rfr_iscdi=true