Evidence map›Paper›PMID 12239287›Full record

ArticleJournal of virology2002

Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki forest viruses with liposomes containing lipid-conjugated heparin.

Jolanda M Smit, Barry-Lee Waarts, Koji Kimata, William B Klimstra, Robert Bittman, Jan Wilschut

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

59 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Pathogens that infect mammalian cells via sulfonated glycosaminoglycans.Frontiers in cellular and infection microbiology · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Entry receptors - the gateway to alphavirus infection.The Journal of clinical investigation · 2023
    Review
  7. Article
  8. Article
  9. Coreceptor functions of cell surface heparan sulfate proteoglycans.American journal of physiology. Cell physiology · 2022
    Review
  10. Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 4 institutions in 3 countries.

Jolanda M SmitMolecular Virology Section, Department of Medical Microbiology, University of Groningen, Ant. Deusinglaan 1, 9713 AV Groningen, The Netherlands.
Barry-Lee Waarts
Koji Kimata
William B Klimstra
Robert Bittman
Jan Wilschut
University of Groningen · NLInstitute for Molecular Science · JPQueens College, CUNY · USUniversity of North Carolina at Chapel Hill · US

Funding

MOLECULAR BASIS OF ALPHAVIRUS NEUROVIRULENCER01AI022186 · NIAID · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI KLIMSTRA, WILLIAM B · 1986 to 2004
$1.6M
STRUCTURAL PROPERTIES OF MEMBRANESR01HL016660 · NHLBI · QUEENS COLLEGE · PI BITTMAN, ROBERT · 1985 to 2003
$1.4M
STRUCTURAL PROPERTIES OF MEMBRANESR37HL016660 · NHLBI · QUEENS COLLEGE · PI BITTMAN, ROBERT · 1986 to 1995
–
NHLBI NIH HHS HL 16660NHLBI NIH HHS R01 HL016660NIAID NIH HHS AI 22186-14NIAID NIH HHS R01 AI022186
6 · The paper itself

Abstract

Passage of Sindbis virus (SIN) in BHK-21 cells has been shown to select for virus mutants with high affinity for the glycosaminoglycan heparan sulfate (HS). Three loci in the viral spike protein E2 (E2:1, E2:70, and E2:114) have been identified that mutate during adaptation and independently confer on the virus the ability to bind to cell surface HS (W. B. Klimstra, K. D. Ryman, and R. E. Johnston, J. Virol. 72:7357-7366, 1998). In this study, we used HS-adapted SIN mutants to evaluate a new model system involving target liposomes containing lipid-conjugated heparin (HepPE) as an HS receptor analog for the virus. HS-adapted SIN, but not nonadapted wild-type SIN TR339, interacted efficiently with HepPE-containing liposomes at neutral pH. Binding was competitively inhibited by soluble heparin. Despite the efficient binding of HS-adapted SIN to HepPE-containing liposomes at neutral pH, there was no fusion under these conditions. Fusion did occur, however, at low pH, consistent with cellular entry of the virus via acidic endosomes. At low pH, wild-type or HS-adapted SIN underwent fusion with liposomes with or without HepPE with similar kinetics, suggesting that interaction with the HS receptor analog at neutral pH has little influence on subsequent fusion of SIN at low pH. Finally, Semliki Forest virus (SFV), passaged frequently on BHK-21 cells, also interacted efficiently with HepPE-containing liposomes, indicating that SFV, like other alphaviruses, readily adapts to cell surface HS. In conclusion, the liposomal model system presented in this paper may serve as a novel tool for the study of receptor interactions and membrane fusion properties of HS-interacting enveloped viruses.

Indexed as

Adaptation, PhysiologicalAnimalsCell LineCholesterolCricetinaeHeparan SulfateHeparinLiposomesMembrane FusionPhosphatidylcholinesPhosphatidylethanolaminesPyrenesSemliki forest virusSindbis VirusSphingomyelinsTrypsin6-photocholesterolCholesterolHeparan SulfateHeparinLiposomesPhosphatidylcholinesPhosphatidylethanolaminesPyrenesSphingomyelinsTrypsin

Identifiers

PMID12239287
PMCPMC136541
OpenAlexW2153927476

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.