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Proteomic analysis of purified turkey adenovirus 3 virions
Turkey adenovirus 3 (TAdV-3) causes high mortality and significant economic losses to the turkey industry. However, little is known about the molecular determinants required for viral replication and pathogenesis. Moreover, TAdV-3 does not grow well in cell culture, thus detailed structural studies...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4497381/ https://www.ncbi.nlm.nih.gov/pubmed/26159706 http://dx.doi.org/10.1186/s13567-015-0214-z |
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author | Kumar, Pankaj van den Hurk, Jan Ayalew, Lisanework E. Gaba, Amit Tikoo, Suresh K. |
author_facet | Kumar, Pankaj van den Hurk, Jan Ayalew, Lisanework E. Gaba, Amit Tikoo, Suresh K. |
author_sort | Kumar, Pankaj |
collection | PubMed |
description | Turkey adenovirus 3 (TAdV-3) causes high mortality and significant economic losses to the turkey industry. However, little is known about the molecular determinants required for viral replication and pathogenesis. Moreover, TAdV-3 does not grow well in cell culture, thus detailed structural studies of the infectious particle is particularly challenging. To develop a better understanding of virus-host interactions, we performed a comprehensive proteomic analysis of proteinase K treated purified TAdV-3 virions isolated from spleens of infected turkeys, by utilizing one-dimensional liquid chromatography mass spectrometry. Our analysis resulted in the identification of 13 viral proteins associated with TAdV-3 virions including a novel uncharacterized TaV3gp04 protein. Further, we detected 18 host proteins in purified virions, many of which are involved in cell-to cell spread, cytoskeleton dynamics and virus replication. Notably, seven of these host proteins have not yet been reported to be present in any other purified virus. In addition, five of these proteins are known antiviral host restriction factors. The availability of reagents allowed us to identify two cellular proteins (collagen alpha-1 (VI) chain and haemoglobin) in the purified TAdV-3 preparations. These results represent the first comprehensive proteomic profile of TAdV-3 and may provide information for illustrating TAdV-3 replication and pathogenesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-015-0214-z) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4497381 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-44973812015-07-10 Proteomic analysis of purified turkey adenovirus 3 virions Kumar, Pankaj van den Hurk, Jan Ayalew, Lisanework E. Gaba, Amit Tikoo, Suresh K. Vet Res Research Article Turkey adenovirus 3 (TAdV-3) causes high mortality and significant economic losses to the turkey industry. However, little is known about the molecular determinants required for viral replication and pathogenesis. Moreover, TAdV-3 does not grow well in cell culture, thus detailed structural studies of the infectious particle is particularly challenging. To develop a better understanding of virus-host interactions, we performed a comprehensive proteomic analysis of proteinase K treated purified TAdV-3 virions isolated from spleens of infected turkeys, by utilizing one-dimensional liquid chromatography mass spectrometry. Our analysis resulted in the identification of 13 viral proteins associated with TAdV-3 virions including a novel uncharacterized TaV3gp04 protein. Further, we detected 18 host proteins in purified virions, many of which are involved in cell-to cell spread, cytoskeleton dynamics and virus replication. Notably, seven of these host proteins have not yet been reported to be present in any other purified virus. In addition, five of these proteins are known antiviral host restriction factors. The availability of reagents allowed us to identify two cellular proteins (collagen alpha-1 (VI) chain and haemoglobin) in the purified TAdV-3 preparations. These results represent the first comprehensive proteomic profile of TAdV-3 and may provide information for illustrating TAdV-3 replication and pathogenesis. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-015-0214-z) contains supplementary material, which is available to authorized users. BioMed Central 2015-07-09 2015 /pmc/articles/PMC4497381/ /pubmed/26159706 http://dx.doi.org/10.1186/s13567-015-0214-z Text en © Kumar et al. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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 Article Kumar, Pankaj van den Hurk, Jan Ayalew, Lisanework E. Gaba, Amit Tikoo, Suresh K. Proteomic analysis of purified turkey adenovirus 3 virions |
title | Proteomic analysis of purified turkey adenovirus 3 virions |
title_full | Proteomic analysis of purified turkey adenovirus 3 virions |
title_fullStr | Proteomic analysis of purified turkey adenovirus 3 virions |
title_full_unstemmed | Proteomic analysis of purified turkey adenovirus 3 virions |
title_short | Proteomic analysis of purified turkey adenovirus 3 virions |
title_sort | proteomic analysis of purified turkey adenovirus 3 virions |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4497381/ https://www.ncbi.nlm.nih.gov/pubmed/26159706 http://dx.doi.org/10.1186/s13567-015-0214-z |
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