Evidence map›Paper›PMID 18786999›Full record

ArticleJournal of virology2008

The measles virus fusion protein transmembrane region modulates availability of an active glycoprotein complex and fusion efficiency.

Michael D Mühlebach, Vincent H J Leonard, Roberto Cattaneo

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Syncytia Formation in Oncolytic Virotherapy.Molecular therapy oncolytics · 2019
    Review
  6. Article
  7. Review
  8. Review
  9. Measles virus: Background and oncolytic virotherapy.Biochemistry and biophysics reports · 2018
    Review
  10. Frontiers in microbiology · 2018
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. MicroRNA-sensitive oncolytic measles viruses for cancer-specific vector tropism.Molecular therapy : the journal of the American Society of Gene Therapy · 2011
    Article
  20. Article
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

3 authors at 1 institution in 2 countries.

Michael D MühlebachMayo Clinic, Department of Molecular Medicine, 200 First Street SW, Rochester, MN 55905, USA.
Vincent H J Leonard
Roberto Cattaneo
Mayo Clinic · US

Funding

Measles Virus Entry: Engagement of the Receptors and Infection ProgressionR01CA090636 · NCI · MAYO CLINIC ROCHESTER · PI CATTANEO, ROBERTO B. · 2002 to 2011
$2.4M
NCI NIH HHS R01 CA090636NCI NIH HHS R01 CA90636
6 · The paper itself

Abstract

The glycoprotein complex of paramyxoviruses mediates receptor binding and membrane fusion. In particular, the measles virus (MV) fusion (F) protein executes membrane fusion, after receptor binding by the hemagglutinin (H) protein. Structures and single amino acids influencing fusion function have been identified in the F-protein ectodomain and cytoplasmic tail, but not in its transmembrane (TM) region. Since this region influences function of the envelope proteins of other viruses, we examined its role in the MV F protein. Alanine-scanning mutagenesis revealed that an F protein with a single mutation of a central TM region leucine (L507A) was more fusogenic than the unmodified F protein while retaining similar kinetics of proteolytic processing. In contrast, substitution of residues located near the edges of the lipid bilayer reduced fusion activity. This was true not only when the mutated F proteins were coexpressed with H but also in the context of infections with recombinant viruses. Analysis of the H-F complexes with reduced fusion activities revealed that more precursor (F(0)) than activated (F(1+2)) protein coprecipitated with H. In contrast, in complexes with enhanced fusion activity, including H-F(L507A), the F(0)/F(1+2) ratio shifted toward F(1+2). Thus, fusion activity correlated with an active F-H protein complex, and the MV F protein TM region modulated availability of this complex.

Indexed as

Virus AttachmentVirus InternalizationAmino Acid SubstitutionAnimalsChlorocebus aethiopsHemagglutininsMeasles virusMutagenesis, Site-DirectedReceptors, VirusVero CellsViral Fusion ProteinsHemagglutininsReceptors, VirusViral Fusion Proteins

Identifiers

PMID18786999
PMCPMC2573273
OpenAlexW2127446275

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.