Evidence map›Paper›PMID 15308701›Full record

ArticleJournal of virology2004

Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head.

Nicolas Massé, Michelle Ainouze, Benjamin Néel, T Fabian Wild, Robin Buckland, Johannes P M Langedijk

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In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.3field-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

46 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
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  4. 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
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  9. Review
  10. Review
  11. Article
  12. Measles Vaccine.Viral immunology · 2018
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. [Advances in measles virus for cancer therapy].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2015
    Article
  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

6 authors at 2 institutions in 2 countries.

Nicolas MasséMolecular Basis of Paramyxovirus Entry, INSERM U404, Immunité et Vaccination, CERVI, IFR 128 Biosciences Lyon-Gerland, Lyon, France.
Michelle Ainouze
Benjamin Néel
T Fabian Wild
Robin Buckland
Johannes P M Langedijk
Inserm · FRPepscan (Netherlands) · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Measles virus hemagglutinin (MVH) residues potentially responsible for attachment to the wild-type (wt) MV receptor SLAM (CD150) have been identified and localized on the MVH globular head by reference to a revised hypothetical structural model for MVH (www.pepscan.nl/downloads/measlesH.pdb). We show that the mutation of five charged MVH residues which are conserved among morbillivirus H proteins has major effects on both SLAM downregulation and SLAM-dependent fusion. In the three-dimensional surface representation of the structural model, three of these residues (D505, D507, and R533) align the rim on one side of the cavity on the top surface of the MVH globular head and form the basis of a single continuous site that overlaps with the 546-548-549 CD46 binding site. We show that the overlapping sites fall within the footprint of an anti-MVH monoclonal antibody that neutralizes both wt and laboratory-vaccine MV strains and whose epitope contains R533. Our study does not exclude the possibility that Y481 binds CD46 directly but suggests that the N481Y mutation of wt MVH could influence, at a distance, the conformation of the overlapping sites so that affinity to CD46 increases. The relevance of these results to present concepts of MV receptor usage is discussed, and an explanation is proposed as to why morbillivirus attachment proteins are H, whereas those from the other paramyxoviruses are HN (hemagglutinin-neuraminidase).

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, ViralAntigens, CDBinding SitesCell LineDown-RegulationEpitopesGlycoproteinsHeLa CellsHemagglutinins, ViralHumansImmunoglobulinsMeasles virusMembrane Cofactor ProteinAntibodies, MonoclonalAntibodies, ViralAntigens, CDCD46 protein, humanEpitopesGlycoproteinsHemagglutinins, ViralImmunoglobulinsMembrane Cofactor ProteinMembrane GlycoproteinsReceptors, Cell SurfaceReceptors, VirusSignaling Lymphocytic Activation Molecule Family Member 1SLAMF1 protein, human

Identifiers

PMID15308701
PMCPMC506930
OpenAlexW2054979198

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.