Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions
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-...
Autores principales: | , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770495/ https://www.ncbi.nlm.nih.gov/pubmed/19835589 http://dx.doi.org/10.1186/1743-422X-6-168 |
_version_ | 1782173669295915008 |
---|---|
author | Ushijima, Yoko Goshima, Fumi Kimura, Hiroshi Nishiyama, Yukihiro |
author_facet | Ushijima, Yoko Goshima, Fumi Kimura, Hiroshi Nishiyama, Yukihiro |
author_sort | Ushijima, Yoko |
collection | PubMed |
description | 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 throughout the cytoplasm. Moreover, UL56 relocalized Nedd4 to the vesicles in cells transiently expressing UL56 and in cells infected with HSV-2. We also investigated whether UL56 influenced the efficiency of viral replication, and found that extracellular infectious viruses were reduced in the absence of UL56. CONCLUSION: These data suggest that UL56 regulates Nedd4 and functions to facilitate the cytoplasmic transport of virions from TGN to the plasma membrane and/or release of virions from the cell surface. |
format | Text |
id | pubmed-2770495 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-27704952009-10-30 Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions Ushijima, Yoko Goshima, Fumi Kimura, Hiroshi Nishiyama, Yukihiro Virol J Research 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 throughout the cytoplasm. Moreover, UL56 relocalized Nedd4 to the vesicles in cells transiently expressing UL56 and in cells infected with HSV-2. We also investigated whether UL56 influenced the efficiency of viral replication, and found that extracellular infectious viruses were reduced in the absence of UL56. CONCLUSION: These data suggest that UL56 regulates Nedd4 and functions to facilitate the cytoplasmic transport of virions from TGN to the plasma membrane and/or release of virions from the cell surface. BioMed Central 2009-10-16 /pmc/articles/PMC2770495/ /pubmed/19835589 http://dx.doi.org/10.1186/1743-422X-6-168 Text en Copyright © 2009 Ushijima et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 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. |
spellingShingle | Research Ushijima, Yoko Goshima, Fumi Kimura, Hiroshi Nishiyama, Yukihiro Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title | Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title_full | Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title_fullStr | Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title_full_unstemmed | Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title_short | Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions |
title_sort | herpes simplex virus type 2 tegument protein ul56 relocalizes ubiquitin ligase nedd4 and has a role in transport and/or release of virions |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770495/ https://www.ncbi.nlm.nih.gov/pubmed/19835589 http://dx.doi.org/10.1186/1743-422X-6-168 |
work_keys_str_mv | AT ushijimayoko herpessimplexvirustype2tegumentproteinul56relocalizesubiquitinligasenedd4andhasaroleintransportandorreleaseofvirions AT goshimafumi herpessimplexvirustype2tegumentproteinul56relocalizesubiquitinligasenedd4andhasaroleintransportandorreleaseofvirions AT kimurahiroshi herpessimplexvirustype2tegumentproteinul56relocalizesubiquitinligasenedd4andhasaroleintransportandorreleaseofvirions AT nishiyamayukihiro herpessimplexvirustype2tegumentproteinul56relocalizesubiquitinligasenedd4andhasaroleintransportandorreleaseofvirions |