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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...

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Autores principales: Striebinger, Hannah, Funk, Christina, Raschbichler, Verena, Bailer, Susanne M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
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.
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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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