Proteomic analysis of the EhV-86 virion

<p>Abstract</p> <p>Background</p> <p><it>Emiliania huxleyi </it>virus 86 (EhV-86) is the type species of the genus <it>Coccolithovirus </it>within the family <it>Phycodnaviridae</it>. The fully sequenced 407,339 bp genome is predicted...

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Main Authors: Lilley Kathryn S, Howard Julie A, Allen Michael J, Wilson William H
Format: Article
Language:English
Published: BMC 2008-03-01
Series:Proteome Science
Online Access:http://www.proteomesci.com/content/6/1/11
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spelling doaj-c91e9af90c4a44959063307801f848d72020-11-24T21:15:33ZengBMCProteome Science1477-59562008-03-01611110.1186/1477-5956-6-11Proteomic analysis of the EhV-86 virionLilley Kathryn SHoward Julie AAllen Michael JWilson William H<p>Abstract</p> <p>Background</p> <p><it>Emiliania huxleyi </it>virus 86 (EhV-86) is the type species of the genus <it>Coccolithovirus </it>within the family <it>Phycodnaviridae</it>. The fully sequenced 407,339 bp genome is predicted to encode 473 protein coding sequences (CDSs) and is the largest <it>Phycodnaviridae </it>sequenced to date. The majority of EhV-86 CDSs exhibit no similarity to proteins in the public databases.</p> <p>Results</p> <p>Proteomic analysis by 1-DE and then LC-MS/MS determined that the virion of EhV-86 is composed of at least 28 proteins, 23 of which are predicted to be membrane proteins. Besides the major capsid protein, putative function can be assigned to 4 other components of the virion: two lectin proteins, a thioredoxin and a serine/threonine protein kinase.</p> <p>Conclusion</p> <p>This study represents the first steps toward the identification of the protein components that make up the EhV-86 virion. Aside from the major capsid protein, whose function in the virion is well known and defined, the nature of the other proteins suggest roles involved with viral budding, caspase activation, signalling, anti-oxidation, virus adsorption and host range determination.</p> http://www.proteomesci.com/content/6/1/11
collection DOAJ
language English
format Article
sources DOAJ
author Lilley Kathryn S
Howard Julie A
Allen Michael J
Wilson William H
spellingShingle Lilley Kathryn S
Howard Julie A
Allen Michael J
Wilson William H
Proteomic analysis of the EhV-86 virion
Proteome Science
author_facet Lilley Kathryn S
Howard Julie A
Allen Michael J
Wilson William H
author_sort Lilley Kathryn S
title Proteomic analysis of the EhV-86 virion
title_short Proteomic analysis of the EhV-86 virion
title_full Proteomic analysis of the EhV-86 virion
title_fullStr Proteomic analysis of the EhV-86 virion
title_full_unstemmed Proteomic analysis of the EhV-86 virion
title_sort proteomic analysis of the ehv-86 virion
publisher BMC
series Proteome Science
issn 1477-5956
publishDate 2008-03-01
description <p>Abstract</p> <p>Background</p> <p><it>Emiliania huxleyi </it>virus 86 (EhV-86) is the type species of the genus <it>Coccolithovirus </it>within the family <it>Phycodnaviridae</it>. The fully sequenced 407,339 bp genome is predicted to encode 473 protein coding sequences (CDSs) and is the largest <it>Phycodnaviridae </it>sequenced to date. The majority of EhV-86 CDSs exhibit no similarity to proteins in the public databases.</p> <p>Results</p> <p>Proteomic analysis by 1-DE and then LC-MS/MS determined that the virion of EhV-86 is composed of at least 28 proteins, 23 of which are predicted to be membrane proteins. Besides the major capsid protein, putative function can be assigned to 4 other components of the virion: two lectin proteins, a thioredoxin and a serine/threonine protein kinase.</p> <p>Conclusion</p> <p>This study represents the first steps toward the identification of the protein components that make up the EhV-86 virion. Aside from the major capsid protein, whose function in the virion is well known and defined, the nature of the other proteins suggest roles involved with viral budding, caspase activation, signalling, anti-oxidation, virus adsorption and host range determination.</p>
url http://www.proteomesci.com/content/6/1/11
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AT allenmichaelj proteomicanalysisoftheehv86virion
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