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Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets

OBJECTIVE: Human adenoviruses are small double stranded DNA viruses that provoke vast array of human diseases. Next generation sequencing techniques increase genomic data of HAdV rapidly, which increase their serotypes. The complete genome sequence of human adenovirus shows that it contains large am...

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Autores principales: Naveed, Muhammad, Tehreem, Sana, Usman, Muhammad, Chaudhry, Zoma, Abbas, Ghulam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719520/
https://www.ncbi.nlm.nih.gov/pubmed/29212526
http://dx.doi.org/10.1186/s13104-017-2992-z
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author Naveed, Muhammad
Tehreem, Sana
Usman, Muhammad
Chaudhry, Zoma
Abbas, Ghulam
author_facet Naveed, Muhammad
Tehreem, Sana
Usman, Muhammad
Chaudhry, Zoma
Abbas, Ghulam
author_sort Naveed, Muhammad
collection PubMed
description OBJECTIVE: Human adenoviruses are small double stranded DNA viruses that provoke vast array of human diseases. Next generation sequencing techniques increase genomic data of HAdV rapidly, which increase their serotypes. The complete genome sequence of human adenovirus shows that it contains large amount of proteins with unknown cellular or biochemical function, known as hypothetical proteins. Hence, it is indispensable to functionally and structurally annotate these proteins to get better understanding of the novel drug targets. The purpose was the characterization of 38 randomly retrieved hypothetical proteins through determination of their physiochemical properties, subcellular localization, function, structure and ligand binding sites using various sequence and structure based bioinformatics tools. RESULTS: Function of six hypothetical proteins P03269, P03261, P03263, Q83127, Q1L4D7 and I6LEV1 were predicted confidently and then used further for structure analysis. We found that these proteins may act as DNA terminal protein, DNA polymerase, DNA binding protein, adenovirus E3 region protein CR1 and adenoviral protein L1. Functional and structural annotation leading to detection of binding sites by means of docking analysis can indicate potential target for therapeutics to defeat adenoviral infection. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13104-017-2992-z) contains supplementary material, which is available to authorized users.
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spelling pubmed-57195202017-12-08 Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets Naveed, Muhammad Tehreem, Sana Usman, Muhammad Chaudhry, Zoma Abbas, Ghulam BMC Res Notes Research Note OBJECTIVE: Human adenoviruses are small double stranded DNA viruses that provoke vast array of human diseases. Next generation sequencing techniques increase genomic data of HAdV rapidly, which increase their serotypes. The complete genome sequence of human adenovirus shows that it contains large amount of proteins with unknown cellular or biochemical function, known as hypothetical proteins. Hence, it is indispensable to functionally and structurally annotate these proteins to get better understanding of the novel drug targets. The purpose was the characterization of 38 randomly retrieved hypothetical proteins through determination of their physiochemical properties, subcellular localization, function, structure and ligand binding sites using various sequence and structure based bioinformatics tools. RESULTS: Function of six hypothetical proteins P03269, P03261, P03263, Q83127, Q1L4D7 and I6LEV1 were predicted confidently and then used further for structure analysis. We found that these proteins may act as DNA terminal protein, DNA polymerase, DNA binding protein, adenovirus E3 region protein CR1 and adenoviral protein L1. Functional and structural annotation leading to detection of binding sites by means of docking analysis can indicate potential target for therapeutics to defeat adenoviral infection. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13104-017-2992-z) contains supplementary material, which is available to authorized users. BioMed Central 2017-12-06 /pmc/articles/PMC5719520/ /pubmed/29212526 http://dx.doi.org/10.1186/s13104-017-2992-z Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Note
Naveed, Muhammad
Tehreem, Sana
Usman, Muhammad
Chaudhry, Zoma
Abbas, Ghulam
Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title_full Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title_fullStr Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title_full_unstemmed Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title_short Structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
title_sort structural and functional annotation of hypothetical proteins of human adenovirus: prioritizing the novel drug targets
topic Research Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719520/
https://www.ncbi.nlm.nih.gov/pubmed/29212526
http://dx.doi.org/10.1186/s13104-017-2992-z
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