Evidence map›Paper›PMID 26459807›Full record

ArticleTraffic (Copenhagen, Denmark)2016

HSV-1 Glycoproteins Are Delivered to Virus Assembly Sites Through Dynamin-Dependent Endocytosis.

Anna Albecka, Romain F Laine, Anne F J Janssen, Clemens F Kaminski, Colin M Crump

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.7field-weighted citation impact, top 7% of its field
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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. The Procaine-Based ProcClusterInternational journal of molecular sciences · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. LIVE-CELL FLUORESCENCE MICROSCOPY OF HSV-1 CELLULAR EGRESS BY EXOCYTOSIS.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. HSV-1 Cytoplasmic Envelopment and Egress.International journal of molecular sciences · 2020
    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

5 authors at 1 institution in 1 country.

Anna AlbeckaDivision of Virology, Department of Pathology, Cambridge University, Cambridge, CB2 1QP, UK.
Romain F LaineLaser Analytics Group, Department of Chemical Engineering and Biotechnology, Cambridge University, Cambridge, CB2 3RA, UK.
Anne F J JanssenDivision of Virology, Department of Pathology, Cambridge University, Cambridge, CB2 1QP, UK.
Clemens F KaminskiLaser Analytics Group, Department of Chemical Engineering and Biotechnology, Cambridge University, Cambridge, CB2 3RA, UK.
Colin M CrumpDivision of Virology, Department of Pathology, Cambridge University, Cambridge, CB2 1QP, UK.ORCID http://orcid.org/0000-0001-9918-9998
University of Cambridge · GB

Funding

Medical Research Council MR/K015850/1
6 · The paper itself

Abstract

Herpes simplex virus-1 (HSV-1) is a large enveloped DNA virus that belongs to the family of Herpesviridae. It has been recently shown that the cytoplasmic membranes that wrap the newly assembled capsids are endocytic compartments derived from the plasma membrane. Here, we show that dynamin-dependent endocytosis plays a major role in this process. Dominant-negative dynamin and clathrin adaptor AP180 significantly decrease virus production. Moreover, inhibitors targeting dynamin and clathrin lead to a decreased transport of glycoproteins to cytoplasmic capsids, confirming that glycoproteins are delivered to assembly sites via endocytosis. We also show that certain combinations of glycoproteins colocalize with each other and with the components of clathrin-dependent and -independent endocytosis pathways. Importantly, we demonstrate that the uptake of neutralizing antibodies that bind to glycoproteins when they become exposed on the cell surface during virus particle assembly leads to the production of non-infectious HSV-1. Our results demonstrate that transport of viral glycoproteins to the plasma membrane prior to endocytosis is the major route by which these proteins are localized to the cytoplasmic virus assembly compartments. This highlights the importance of endocytosis as a major protein-sorting event during HSV-1 envelopment.

Indexed as

EndocytosisVirus AssemblyAnimalsChlorocebus aethiopsClathrinCOS CellsDynaminsGlycoproteinsHerpesvirus 1, HumanHumansMonomeric Clathrin Assembly ProteinsProtein TransportVero CellsViral ProteinsClathrinclathrin assembly protein AP180DynaminsGlycoproteinsMonomeric Clathrin Assembly ProteinsViral ProteinsdSTORMdynaminendocytosisglycoproteinHSVvirus assembly

Identifiers

PMID26459807
PMCPMC4745000
OpenAlexW2104040724

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.