Evidence map›Paper›PMID 23760251›Full record

ArticleJournal of virology2013

The measles virus hemagglutinin β-propeller head β4-β5 hydrophobic groove governs functional interactions with nectin-4 and CD46 but not those with the signaling lymphocytic activation molecule.

Mathieu Mateo, Chanakha K Navaratnarajah, Sabriya Syed, Roberto Cattaneo

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. FeMV is a cathepsin-dependent unique morbillivirus infecting the kidneys of domestic cats.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. WeakJournal of virology · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Mathieu MateoDepartment of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.
Chanakha K Navaratnarajah
Sabriya Syed
Roberto Cattaneo
Mayo Clinic · USUniversity of Rochester · US

Funding

Immunosuppression and Innate Immunity Control by MorbillivirusesR01AI063476 · NIAID · MAYO CLINIC ROCHESTER · PI CATTANEO, ROBERTO B. · 2005 to 2014
$3.2M
NIAID NIH HHS R01 AI063476
6 · The paper itself

Abstract

Wild-type measles virus (MV) strains use the signaling lymphocytic activation molecule (SLAM; CD150) and the adherens junction protein nectin-4 (poliovirus receptor-like 4 [PVRL4]) as receptors. Vaccine MV strains have adapted to use ubiquitous membrane cofactor protein (MCP; CD46) in addition. Recently solved cocrystal structures of the MV attachment protein (hemagglutinin [H]) with each receptor indicate that all three bind close to a hydrophobic groove located between blades 4 and 5 (β4-β5 groove) of the H protein β-propeller head. We used this structural information to focus our analysis of the functional footprints of the three receptors on vaccine MV H. We mutagenized this protein and tested the ability of individual mutants to support cell fusion through each receptor. The results highlighted a strong overlap between the functional footprints of nectin-4 and CD46 but not those of SLAM. A soluble form of nectin-4 abolished vaccine MV entry in nectin-4- and CD46-expressing cells but only reduced entry through SLAM. Analyses of the binding kinetics of an H mutant with the three receptors revealed that a single substitution in the β4-β5 groove drastically reduced nectin-4 and CD46 binding while minimally altering SLAM binding. We also generated recombinant viruses and analyzed their infections in cells expressing individual receptors. Introduction of a single substitution into the hydrophobic pocket affected entry through both nectin-4 and CD46 but not through SLAM. Thus, while nectin-4 and CD46 interact functionally with the H protein β4-β5 hydrophobic groove, SLAM merely covers it. This has implications for vaccine and antiviral strategies.

Indexed as

Host-Pathogen InteractionsVirus InternalizationAnimalsAntigens, CDCell Adhesion MoleculesChlorocebus aethiopsDNA Mutational AnalysisMeasles virusMembrane Cofactor ProteinNectinsProtein BindingProtein Interaction MappingReceptors, Cell SurfaceReceptors, VirusSignaling Lymphocytic Activation Molecule Family Member 1Vero CellsAntigens, CDCD46 protein, humanCell Adhesion MoleculesMembrane Cofactor ProteinNECTIN4 protein, humanNectinsReceptors, Cell SurfaceReceptors, VirusSignaling Lymphocytic Activation Molecule Family Member 1SLAMF1 protein, humanViral Proteins

Identifiers

PMID23760251
PMCPMC3754078
OpenAlexW2068839843

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.