The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.

There is enormous interest in studying HIV pathogenesis for improving the treatment of patients with HIV infection. HIV infection has become one of the best-studied systems for understanding how a virus can hijack a cell. To help facilitate discovery, we previously built HIVToolbox, a web system for...

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Main Authors: David P Sargeant, Sandeep Deverasetty, Christy L Strong, Izua J Alaniz, Alexandria Bartlett, Nicholas R Brandon, Steven B Brooks, Frederick A Brown, Flaviona Bufi, Monika Chakarova, Roxanne P David, Karlyn M Dobritch, Horacio P Guerra, Michael W Hedden, Rma Kumra, Kelvy S Levitt, Kiran R Mathew, Ray Matti, Dorothea Q Maza, Sabyasachy Mistry, Nemanja Novakovic, Austin Pomerantz, Josue Portillo, Timothy F Rafalski, Viraj R Rathnayake, Noura Rezapour, Sarah Songao, Sean L Tuggle, Sandy Yousif, David I Dorsky, Martin R Schiller
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4041786?pdf=render
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author David P Sargeant
Sandeep Deverasetty
Christy L Strong
Izua J Alaniz
Alexandria Bartlett
Nicholas R Brandon
Steven B Brooks
Frederick A Brown
Flaviona Bufi
Monika Chakarova
Roxanne P David
Karlyn M Dobritch
Horacio P Guerra
Michael W Hedden
Rma Kumra
Kelvy S Levitt
Kiran R Mathew
Ray Matti
Dorothea Q Maza
Sabyasachy Mistry
Nemanja Novakovic
Austin Pomerantz
Josue Portillo
Timothy F Rafalski
Viraj R Rathnayake
Noura Rezapour
Sarah Songao
Sean L Tuggle
Sandy Yousif
David I Dorsky
Martin R Schiller
author_facet David P Sargeant
Sandeep Deverasetty
Christy L Strong
Izua J Alaniz
Alexandria Bartlett
Nicholas R Brandon
Steven B Brooks
Frederick A Brown
Flaviona Bufi
Monika Chakarova
Roxanne P David
Karlyn M Dobritch
Horacio P Guerra
Michael W Hedden
Rma Kumra
Kelvy S Levitt
Kiran R Mathew
Ray Matti
Dorothea Q Maza
Sabyasachy Mistry
Nemanja Novakovic
Austin Pomerantz
Josue Portillo
Timothy F Rafalski
Viraj R Rathnayake
Noura Rezapour
Sarah Songao
Sean L Tuggle
Sandy Yousif
David I Dorsky
Martin R Schiller
author_sort David P Sargeant
collection DOAJ
description There is enormous interest in studying HIV pathogenesis for improving the treatment of patients with HIV infection. HIV infection has become one of the best-studied systems for understanding how a virus can hijack a cell. To help facilitate discovery, we previously built HIVToolbox, a web system for visual data mining. The original HIVToolbox integrated information for HIV protein sequence, structure, functional sites, and sequence conservation. This web system has been used for almost 40,000 searches. We report improvements to HIVToolbox including new functions and workflows, data updates, and updates for ease of use. HIVToolbox2, is an improvement over HIVToolbox with new functions. HIVToolbox2 has new functionalities focused on HIV pathogenesis including drug-binding sites, drug-resistance mutations, and immune epitopes. The integrated, interactive view enables visual mining to generate hypotheses that are not readily revealed by other approaches. Most HIV proteins form multimers, and there are posttranslational modification and protein-protein interaction sites at many of these multimerization interfaces. Analysis of protease drug binding sites reveals an anatomy of drug resistance with different types of drug-resistance mutations regionally localized on the surface of protease. Some of these drug-resistance mutations have a high prevalence in specific HIV-1 M subtypes. Finally, consolidation of Tat functional sites reveals a hotspot region where there appear to be 30 interactions or posttranslational modifications. A cursory analysis with HIVToolbox2 has helped to identify several global patterns for HIV proteins. An initial analysis with this tool identifies homomultimerization of almost all HIV proteins, functional sites that overlap with multimerization sites, a global drug resistance anatomy for HIV protease, and specific distributions of some DRMs in specific HIV M subtypes. HIVToolbox2 is an open-access web application available at [http://hivtoolbox2.bio-toolkit.com].
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spelling doaj.art-50992c4abf2f4d018d2567fbf1d4b0352022-12-22T02:04:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0196e9881010.1371/journal.pone.0098810The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.David P SargeantSandeep DeverasettyChristy L StrongIzua J AlanizAlexandria BartlettNicholas R BrandonSteven B BrooksFrederick A BrownFlaviona BufiMonika ChakarovaRoxanne P DavidKarlyn M DobritchHoracio P GuerraMichael W HeddenRma KumraKelvy S LevittKiran R MathewRay MattiDorothea Q MazaSabyasachy MistryNemanja NovakovicAustin PomerantzJosue PortilloTimothy F RafalskiViraj R RathnayakeNoura RezapourSarah SongaoSean L TuggleSandy YousifDavid I DorskyMartin R SchillerThere is enormous interest in studying HIV pathogenesis for improving the treatment of patients with HIV infection. HIV infection has become one of the best-studied systems for understanding how a virus can hijack a cell. To help facilitate discovery, we previously built HIVToolbox, a web system for visual data mining. The original HIVToolbox integrated information for HIV protein sequence, structure, functional sites, and sequence conservation. This web system has been used for almost 40,000 searches. We report improvements to HIVToolbox including new functions and workflows, data updates, and updates for ease of use. HIVToolbox2, is an improvement over HIVToolbox with new functions. HIVToolbox2 has new functionalities focused on HIV pathogenesis including drug-binding sites, drug-resistance mutations, and immune epitopes. The integrated, interactive view enables visual mining to generate hypotheses that are not readily revealed by other approaches. Most HIV proteins form multimers, and there are posttranslational modification and protein-protein interaction sites at many of these multimerization interfaces. Analysis of protease drug binding sites reveals an anatomy of drug resistance with different types of drug-resistance mutations regionally localized on the surface of protease. Some of these drug-resistance mutations have a high prevalence in specific HIV-1 M subtypes. Finally, consolidation of Tat functional sites reveals a hotspot region where there appear to be 30 interactions or posttranslational modifications. A cursory analysis with HIVToolbox2 has helped to identify several global patterns for HIV proteins. An initial analysis with this tool identifies homomultimerization of almost all HIV proteins, functional sites that overlap with multimerization sites, a global drug resistance anatomy for HIV protease, and specific distributions of some DRMs in specific HIV M subtypes. HIVToolbox2 is an open-access web application available at [http://hivtoolbox2.bio-toolkit.com].http://europepmc.org/articles/PMC4041786?pdf=render
spellingShingle David P Sargeant
Sandeep Deverasetty
Christy L Strong
Izua J Alaniz
Alexandria Bartlett
Nicholas R Brandon
Steven B Brooks
Frederick A Brown
Flaviona Bufi
Monika Chakarova
Roxanne P David
Karlyn M Dobritch
Horacio P Guerra
Michael W Hedden
Rma Kumra
Kelvy S Levitt
Kiran R Mathew
Ray Matti
Dorothea Q Maza
Sabyasachy Mistry
Nemanja Novakovic
Austin Pomerantz
Josue Portillo
Timothy F Rafalski
Viraj R Rathnayake
Noura Rezapour
Sarah Songao
Sean L Tuggle
Sandy Yousif
David I Dorsky
Martin R Schiller
The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
PLoS ONE
title The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
title_full The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
title_fullStr The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
title_full_unstemmed The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
title_short The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.
title_sort hivtoolbox 2 web system integrates sequence structure function and mutation analysis
url http://europepmc.org/articles/PMC4041786?pdf=render
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