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Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M
The herpes simplex virus type 1 (HSV-1) glycoprotein N (gN/UL49.5) is a type I transmembrane protein conserved throughout the herpesvirus family. gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN are covalently linked by a...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810273/ https://www.ncbi.nlm.nih.gov/pubmed/26999189 http://dx.doi.org/10.3390/v8030083 |
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author | Striebinger, Hannah Funk, Christina Raschbichler, Verena Bailer, Susanne M. |
author_facet | Striebinger, Hannah Funk, Christina Raschbichler, Verena Bailer, Susanne M. |
author_sort | Striebinger, Hannah |
collection | PubMed |
description | The herpes simplex virus type 1 (HSV-1) glycoprotein N (gN/UL49.5) is a type I transmembrane protein conserved throughout the herpesvirus family. gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN are covalently linked by a single disulphide bond formed between cysteine 46 of gN and cysteine 59 of gM. Exit of gN from the endoplasmic reticulum requires the N-terminal core of gM composed of eight transmembrane domains but is independent of the C-terminal extension of gM. Co-transport of gN and gM to the trans Golgi network also occurs upon replacement of conserved cysteines in gM and gN, suggesting that their physical interaction is mediated by covalent and non-covalent forces. Deletion of gN/UL49.5 using bacterial artificial chromosome (BAC) mutagenesis generated mutant viruses with wild-type growth behaviour, while full deletion of gM/UL10 resulted in an attenuated phenotype. Deletion of gN/UL49.5 in conjunction with various gM/UL10 mutants reduced average plaque sizes to the same extent as either single gM/UL10 mutant, indicating that gN is nonessential for the function performed by gM. We propose that gN functions in gM-dependent as well as gM-independent processes during which it is complemented by other viral factors. |
format | Online Article Text |
id | pubmed-4810273 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-48102732016-04-04 Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M Striebinger, Hannah Funk, Christina Raschbichler, Verena Bailer, Susanne M. Viruses Article The herpes simplex virus type 1 (HSV-1) glycoprotein N (gN/UL49.5) is a type I transmembrane protein conserved throughout the herpesvirus family. gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN are covalently linked by a single disulphide bond formed between cysteine 46 of gN and cysteine 59 of gM. Exit of gN from the endoplasmic reticulum requires the N-terminal core of gM composed of eight transmembrane domains but is independent of the C-terminal extension of gM. Co-transport of gN and gM to the trans Golgi network also occurs upon replacement of conserved cysteines in gM and gN, suggesting that their physical interaction is mediated by covalent and non-covalent forces. Deletion of gN/UL49.5 using bacterial artificial chromosome (BAC) mutagenesis generated mutant viruses with wild-type growth behaviour, while full deletion of gM/UL10 resulted in an attenuated phenotype. Deletion of gN/UL49.5 in conjunction with various gM/UL10 mutants reduced average plaque sizes to the same extent as either single gM/UL10 mutant, indicating that gN is nonessential for the function performed by gM. We propose that gN functions in gM-dependent as well as gM-independent processes during which it is complemented by other viral factors. MDPI 2016-03-17 /pmc/articles/PMC4810273/ /pubmed/26999189 http://dx.doi.org/10.3390/v8030083 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Striebinger, Hannah Funk, Christina Raschbichler, Verena Bailer, Susanne M. Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title | Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title_full | Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title_fullStr | Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title_full_unstemmed | Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title_short | Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M |
title_sort | subcellular trafficking and functional relationship of the hsv-1 glycoproteins n and m |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810273/ https://www.ncbi.nlm.nih.gov/pubmed/26999189 http://dx.doi.org/10.3390/v8030083 |
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