Evidence map›Paper›PMID 23651212›Full record

ArticleBiochemistry2013

SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release.

Smita Raghava, Kristina M Giorda, Fabian B Romano, Alejandro P Heuck, Daniel N Hebert

Abstract read
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.5field-weighted citation impact, top 5% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Human polyomaviruses and cancer: an overview.Clinics (Sao Paulo, Brazil) · 2018
    Review
  9. Article
  10. Nuclear Exodus: Herpesviruses Lead the Way.Annual review of virology · 2016
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. 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.

Smita RaghavaDepartment of Biochemistry and Molecular Biology, University of Massachusetts , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.
Kristina M Giorda
Fabian B Romano
Alejandro P Heuck
Daniel N Hebert
University of Massachusetts Amherst · US

Funding

Cellular protein maturation and degradationR01GM086874 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RAUCH, JENNIFER NICOLE · 2009 to 2025
$4.5M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Simian Virus 40 (SV40) uncoating and penetrationR21AI078142 · NIAID · UNIVERSITY OF MASSACHUSETTS AMHERST · PI HEBERT, DANIEL N. · 2008 to 2009
$422k
NIAID NIH HHS AI078142NIAID NIH HHS R21 AI078142NIGMS NIH HHS GM086874NIGMS NIH HHS R01 GM086874NIGMS NIH HHS T32GM00815NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

Nonenveloped viruses are generally released from the cell by the timely lysis of host cell membranes. SV40 has been used as a model virus for the study of the lytic nonenveloped virus life cycle. The expression of SV40 VP4 at later times during infection is concomitant with cell lysis. To investigate the role of VP4 in viral release and its mechanism of action, VP4 was expressed and purified from bacteria as a fusion protein for use in membrane disruption assays. Purified VP4 perforated membranes as demonstrated by the release of fluorescent markers encapsulated within large unilamellar vesicles or liposomes. Dynamic light scattering results revealed that VP4 treatment did not cause membrane lysis or change the size of the liposomes. Liposomes encapsulated with 4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-3-indacene-labeled streptavidin were used to show that VP4 formed stable pores in membranes. These VP4 pores had an inner diameter of 1-5 nm. Asymmetrical liposomes containing pyrene-labeled lipids in the outer monolayer were employed to monitor transbilayer lipid diffusion. Consistent with VP4 forming toroidal pore structures in membranes, VP4 induced transbilayer lipid diffusion or lipid flip-flop. Altogether, these studies support a central role for VP4 acting as a viroporin in the disruption of cellular membranes to trigger SV40 viral release by forming toroidal pores that unite the outer and inner leaflets of membrane bilayers.

Indexed as

Cell MembraneLipid BilayersLiposomesMembranesSimian virus 40Viral Regulatory and Accessory ProteinsVirus ReleaseLipid BilayersLiposomesViral Regulatory and Accessory Proteins

Identifiers

PMID23651212
PMCPMC4235334
OpenAlexW2034479050

What OpenQuestion holds

Textmetadata
LicenceTDM
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.