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Báo cáo khoa học: "Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions | Virology Journal BioMed Central Research Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and or release of virions Yoko Ushijima Fumi Goshima Hiroshi Kimura and Yukihiro Nishiyama Open Access Address Department of Virology Nagoya University Graduate School of Medicine 65 Tsurumai-cho Showa-ku Nagoya 466-8550 Japan Email Yoko Ushijima - ushiy-5@med.nagoya-u.ac.jp Fumi Goshima - fgoshima@med.nagoya-u.ac.jp Hiroshi Kimura - hkimura@med.nagoya-u.ac.jp Yukihiro Nishiyama - ynishiya@med.nagoya-u.ac.jp Corresponding author Published 16 October 2009 Received 4 September 2009 Accepted 16 October 2009 Virology Journal 2009 6 168 doi l0.ll86 I743-422X-6-I68 This article is available from http www.virologyj.com content 6 1 168 2009 Ushijima et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The ubiquitin system functions in a variety of cellular processes including protein turnover protein sorting and trafficking. Many viruses exploit the cellular ubiquitin system to facilitate viral replication. In fact herpes simplex virus HSV encodes a ubiquitin ligase E3 and a de-ubiquitinating enzyme to modify the host s ubiquitin system. We have previously reported HSV type 2 HSV-2 tegument protein UL56 as a putative adaptor protein of neuronal precursor cell-expressed developmentally down-regulated 4 Nedd4 E3 ligase which has been shown to be involved in protein sorting and trafficking. Results In this study we visualized and characterized the dynamic intracellular localization of UL56 and Nedd4 using live-cell imaging and immunofluorescence analysis. UL56 was distributed to cytoplasmic vesicles primarily to the trans-Golgi network TGN and trafficked actively