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Post translational modifications in adenovirus type 2
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Cancer and Vascular Biology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Science for Life Laboratory, SciLifeLab.
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2013 (English)In: Virology, ISSN 0042-6822, E-ISSN 1096-0341, Vol. 447, no 1-2, 104-111 p.Article in journal (Refereed) Published
Abstract [en]

We have combined 2-D SOS-PAGE with liquid chromatography-high resolving mass spectrometry (LC-MS) to explore the proteome of the adenovirus type 2 (Ad2) at the level of post translational modifications (PTMs). The experimental design included in-solution digestion, followed by titanium dioxide enrichment, as well as in-gel digestion of polypeptides after separation of Ad2 capsid proteins by 1-D and 2-D SOS-PAGE. All samples were analyzed using LC-MS with subsequent manual verification of PTM positions. The results revealed new phosphorylation sites that can explain the observed trains of protein spots observed for the pIII, pIIIa and ply proteins. The pin protein was found to be the most highly modified protein with now 18 verified sites of phosphorylation, three sites of nitrated tyrosine and one sulfated tyrosine. Nitrated tyrosines were also identified in pII. Lysine acetylations were detected in pII and pVI. The findings make the Ad2 virion much more complex than hitherto believed. 

Place, publisher, year, edition, pages
2013. Vol. 447, no 1-2, 104-111 p.
Keyword [en]
Adenovirus type 2, Post translational modification analysis, 2-D SOS-PAGE, High resolving mass spectrometry
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-212309DOI: 10.1016/j.virol.2013.08.033ISI: 000326553500011OAI: oai:DiVA.org:uu-212309DiVA: diva2:677704
Available from: 2013-12-10 Created: 2013-12-09 Last updated: 2017-12-06Bibliographically approved

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Lind, Sara BergströmArtemenko, Konstantin A.Elfineh, LioudmilaBergquist, JonasPettersson, Ulf

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