Evidence map›Paper›PMID 11991976›Full record

ArticleJournal of virology2002

Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum.

Ivo C Lorenz, Steven L Allison, Franz X Heinz, Ari Helenius

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 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
12.2field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 255 citations in OpenAlex.

  1. Application of Orthoflavivirus Pseudovirus Technology in Antiviral Research.International journal of molecular sciences · 2026
    Review
  2. An Updated Review of Potential Drug Targets for Japanese Encephalitis.Central nervous system agents in medicinal chemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. pr-independent biogenesis of infectious mature Zika virus particles.bioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Replication is the key barrier during the dual-host adaptation of mosquito-borne flaviviruses.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Review
  20. Article

48 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

4 authors at 2 institutions in 2 countries.

Ivo C LorenzInstitute of Biochemistry, Swiss Federal Institute of Technology, CH-8093 Zürich, Switzerland.
Steven L Allison
Franz X Heinz
Ari Helenius
École Polytechnique Fédérale de Lausanne · CHUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flavivirus envelope proteins are synthesized as part of large polyproteins that are co- and posttranslationally cleaved into their individual chains. To investigate whether the interaction of neighboring proteins within the precursor protein is required to ensure proper maturation of the individual components, we have analyzed the folding of the flavivirus tick-borne encephalitis (TBE) virus envelope glycoproteins prM and E by using a recombinant plasmid expression system and virus-infected cells. When expressed in their polyprotein context, prM and E achieved their native folded structures with half-times of approximately 4 min for prM and about 15 min for E. They formed heterodimeric complexes within a few minutes after synthesis that were required for the final folding of E but not for that of prM. Heterodimers could also be formed in trans when these proteins were coexpressed from separate constructs. When expressed without prM, E could form disulfide bonds but did not express a specific conformational epitope and remained sensitive to reduction by dithiothreitol. This is consistent with a chaperone-like role for prM in the folding of E. PrM was able to achieve its native folded structure without coexpression of E, but signal sequence cleavage at the N terminus was delayed. Our results show that prM is an especially rapidly folding viral glycoprotein, that polyprotein cleavage and folding of the TBE virus envelope proteins occurs in a coordinated sequence of processing steps, and that proper and efficient maturation of prM and E can only be achieved by cosynthesis of these two proteins.

Indexed as

Protein FoldingAnimalsChlorocebus aethiopsCOS CellsDimerizationDithiothreitolEncephalitis Viruses, Tick-BorneHexosaminidasesPolyproteinsProtein PrecursorsRecombinant Fusion ProteinsViral Envelope ProteinsDithiothreitolglycoprotein E, FlavivirusHexosaminidasesPolyproteinsprM protein, FlavivirusProtein PrecursorsRecombinant Fusion ProteinsViral Envelope Proteins

Identifiers

PMID11991976
PMCPMC137023
OpenAlexW2152542121

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.