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Open AccessArticle

Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M

Max von Pettenkofer-Institute, Ludwig-Maximilians-University München, Munich 80336, Germany
Institute for Interfacial Engineering and Plasma Technology IGVP, University of Stuttgart, Stuttgart 70569, Germany
Fraunhofer Institute for Interfacial Engineering and Biotechnology IGB, Stuttgart 70569, Germany
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Andrew Ward
Viruses 2016, 8(3), 83;
Received: 20 September 2015 / Revised: 19 February 2016 / Accepted: 2 March 2016 / Published: 17 March 2016
(This article belongs to the Special Issue Viral Glycoprotein Structure)
PDF [4866 KB, uploaded 17 March 2016]


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. View Full-Text
Keywords: herpesvirus; HSV-1; glycoprotein N; UL49.5; glycoprotein M; UL10 herpesvirus; HSV-1; glycoprotein N; UL49.5; glycoprotein M; UL10

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Striebinger, H.; Funk, C.; Raschbichler, V.; Bailer, S.M. Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M. Viruses 2016, 8, 83.

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