Evidence map›Paper›PMID 26999189›Full record

ArticleViruses2016

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

Hannah Striebinger, Christina Funk, Verena Raschbichler, Susanne M Bailer

Abstract read
In one paragraph

Article in Viruses, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Article
  2. Article
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  5. Article
  6. Review
  7. Review
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Herpes simplex virus Membrane Fusion.Advances in anatomy, embryology, and cell biology · 2017
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Hannah StriebingerMax von Pettenkofer-Institute, Ludwig-Maximilians-University München, Munich 80336, Germany. h.striebinger@yahoo.de.
Christina FunkInstitute for Interfacial Engineering and Plasma Technology IGVP, University of Stuttgart, Stuttgart 70569, Germany. Christina.Funk@igb.fraunhofer.de.
Verena RaschbichlerMax von Pettenkofer-Institute, Ludwig-Maximilians-University München, Munich 80336, Germany. verenarasch@gmail.com.
Susanne M BailerMax von Pettenkofer-Institute, Ludwig-Maximilians-University München, Munich 80336, Germany. Susanne.Bailer@igvp.uni-stuttgart.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Virus AssemblyVirus InternalizationEndoplasmic ReticulumGene DeletionGolgi ApparatusHeLa CellsHerpesvirus 1, HumanHumansMembrane GlycoproteinsProtein BindingProtein TransportViral Matrix ProteinsViral Plaque AssayViral ProteinsMembrane GlycoproteinsUL10 protein, Human herpesvirus 1UL49A protein, Human herpesvirus 2Viral Matrix ProteinsViral Proteinsglycoprotein Mglycoprotein NherpesvirusHSV-1UL10UL49.5

Identifiers

PMID26999189
PMCPMC4810273

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.