Evidence map›Paper›PMID 29414708›Full record

ArticleBiophysical journal2018

Why Enveloped Viruses Need Cores-The Contribution of a Nucleocapsid Core to Viral Budding.

Guillermo R Lázaro, Suchetana Mukhopadhyay, Michael F Hagan

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Current perspectives on alphavirus encapsidation, assembly and budding.Frontiers in cellular and infection microbiology · 2025
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Flaviviruses have imperfect icosahedral symmetry.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  17. Article
  18. Article
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

3 authors at 2 institutions in 1 country.

Guillermo R LázaroMartin Fisher School of Physics, Brandeis University, Waltham, Massachusetts.
Suchetana MukhopadhyayDepartment of Biology, Indiana University, Bloomington, Indiana.
Michael F HaganMartin Fisher School of Physics, Brandeis University, Waltham, Massachusetts. Electronic address: hagan@brandeis.edu.
Brandeis University · USIndiana University Bloomington · US

Funding

Computational modeling of viral capsid and bacterial microcompartment assemblyR01GM108021 · NIGMS · BRANDEIS UNIVERSITY · PI HAGAN, MICHAEL F · 2013 to 2021
$2.7M
NIGMS NIH HHS R01 GM108021
6 · The paper itself

Abstract

During the lifecycle of many enveloped viruses, a nucleocapsid core buds through the cell membrane to acquire an outer envelope of lipid membrane and viral glycoproteins. However, the presence of a nucleocapsid core is not required for assembly of infectious particles. To determine the role of the nucleocapsid core, we develop a coarse-grained computational model with which we investigate budding dynamics as a function of glycoprotein and nucleocapsid interactions, as well as budding in the absence of a nucleocapsid. We find that there is a transition between glycoprotein-directed budding and nucleocapsid-directed budding that occurs above a threshold strength of nucleocapsid interactions. The simulations predict that glycoprotein-directed budding leads to significantly increased size polydispersity and particle polymorphism. This polydispersity can be explained by a theoretical model accounting for the competition between bending energy of the membrane and the glycoprotein shell. The simulations also show that the geometry of a budding particle leads to a barrier to subunit diffusion, which can result in a stalled, partially budded state. We present a phase diagram for this and other morphologies of budded particles. Comparison of these structures against experiments could establish bounds on whether budding is directed by glycoprotein or nucleocapsid interactions. Although our model is motivated by alphaviruses, we discuss implications of our results for other enveloped viruses.

Indexed as

Virus ReleaseCell MembraneGlycoproteinsNucleocapsidProtein TransportSindbis VirusViral ProteinsVirus AssemblyGlycoproteinsViral Proteins

Identifiers

PMID29414708
PMCPMC5985022
OpenAlexW2750386037

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.