Evidence map›Paper›PMID 23273918›Full record

ArticleCell reports2013

Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry.

Kamel El Omari, Oleg Iourin, Karl Harlos, Jonathan M Grimes, David I Stuart

Abstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
–field-weighted citation impact
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

85 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
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  7. Article
  8. Glycoproteins in Viruses.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
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  11. Article
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  13. Article
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  15. Article
  16. Review
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  20. Review

25 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.

Kamel El OmariDivision of Structural Biology, The Wellcome Trust Center for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.
Oleg Iourin
Karl Harlos
Jonathan M Grimes
David I Stuart

Funding

Medical Research Council G1000099Medical Research Council G1100525Wellcome Trust 075491/Z/04Wellcome Trust 090532
6 · The paper itself

Abstract

Enveloped viruses have developed various adroit mechanisms to invade their host cells. This process requires one or more viral envelope glycoprotein to achieve cell attachment and membrane fusion. Members of the Flaviviridae such as flaviviruses possess only one envelope glycoprotein, E, whereas pestiviruses and hepacivirus encode two glycoproteins, E1 and E2. Although E2 is involved in cell attachment, it has been unclear which protein is responsible for membrane fusion. We report the crystal structures of the homodimeric glycoprotein E2 from the pestivirus bovine viral diarrhea virus 1 (BVDV1) at both neutral and low pH. Unexpectedly, BVDV1 E2 does not have a class II fusion protein fold, and at low pH the N-terminal domain is disordered, similarly to the intermediate postfusion state of E2 from sindbis virus, an alphavirus. Our results suggest that the pestivirus and possibly the hepacivirus fusion machinery are unlike any previously observed.

Indexed as

Virus InternalizationAmino Acid SequenceAnimalsCattleConserved SequenceDiarrhea Virus 1, Bovine ViralEpitopesHEK293 CellsHumansModels, MolecularMolecular Sequence DataProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipEpitopesViral Envelope Proteins

Identifiers

PMID23273918
PMCPMC3607223

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.