Evidence map›Paper›PMID 14645552›Full record

ArticleJournal of virology2003

Further evidence that papillomavirus capsids exist in two distinct conformations.

Hans-Christoph Selinka, Tzenan Giroglou, Thorsten Nowak, Neil D Christensen, Martin Sapp

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

82 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Variations in Genes Encoding Human Papillomavirus Binding Receptors and Susceptibility to Cervical Precancer.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2023
    Article
  3. Article
  4. Human Papilloma Virus-Infected Cells.Sub-cellular biochemistry · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Diazadispiroalkane Derivatives Are New Viral Entry Inhibitors.Antimicrobial agents and chemotherapy · 2021
    Article
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22 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Hans-Christoph SelinkaInstitute for Medical Microbiology and Hygiene, University of Mainz, D-55101 Mainz, Germany.
Tzenan Giroglou
Thorsten Nowak
Neil D Christensen
Martin Sapp
Institute of Medical Microbiology and Hygiene · DEJohannes Gutenberg University Mainz · DEPenn State Milton S. Hershey Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell surface heparan sulfate proteoglycans (HSPGs) serve as primary attachment receptors for human papillomaviruses (HPVs). To demonstrate that a biologically functional HPV-receptor interaction is restricted to a specific subset of HSPGs, we first explored the role of HSPG glucosaminoglycan side chain modifications. We demonstrate that HSPG O sulfation is essential for HPV binding and infection, whereas de-N-sulfated heparin interfered with VLP binding but not with HPV pseudoinfection. This points to differences in VLP-HSPG and pseudovirion-HSPG interactions. Interestingly, internalization kinetics of VLPs and pseudovirions, as measured by fluorescence-activated cell sorting analysis, also differ significantly with approximate half times of 3.5 and 7.5 h, respectively. These data suggest that differences in HSPG binding significantly influence postbinding events. We also present evidence that pseudovirions undergo a conformational change after cell attachment. A monoclonal antibody (H33.J3), which displays negligible effectiveness in preattachment neutralization assays, efficiently neutralizes cell-bound virions. However, no difference in H33.J3 binding to pseudovirions and VLPs was observed in enzyme-linked immunosorbent assay and virus capture assays. In contrast to antibody H33.B6, which displays equal efficiencies in pre- and postattachment neutralization assays, H33.J3 does not block VLP binding to heparin, demonstrating that it interferes with steps subsequent to virus binding. Our data strongly suggest that H33.J3 recognizes a conformation-dependent epitope in capsid protein L1, which undergoes a structural change after cell attachment.

Indexed as

Protein ConformationAnimalsAntibodies, MonoclonalAntibodies, ViralCapsidCapsid ProteinsChlorocebus aethiopsCOS CellsEpitopesFlow CytometryHeparan Sulfate ProteoglycansHumansMiceNeutralization TestsPapillomaviridaeReceptors, VirusAntibodies, MonoclonalAntibodies, ViralCapsid ProteinsEpitopesHeparan Sulfate ProteoglycansReceptors, Virus

Identifiers

PMID14645552
PMCPMC296061
OpenAlexW2015974605

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.