Evidence map›Paper›PMID 17567703›Full record

ArticleJournal of virology2007

Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin.

Peter L Delputte, Wander Van Breedam, Iris Delrue, Cornelia Oetke, Paul R Crocker, Hans J Nauwynck

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

2 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

6 authors at 3 institutions in 2 countries.

Peter L DelputteLaboratory of Virology, Department Virology, Parasitology, and Immunology, Ghent University, Salisburylaan 133, B-9820 Merelbeke, Belgium. peter.delputte@UGent.be
Wander Van Breedam
Iris Delrue
Cornelia Oetke
Paul R Crocker
Hans J Nauwynck
Ghent University · BEUniversity of Dundee · GBWellcome Trust · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). To investigate the importance of pSn sialic acid-binding activity for PRRSV infection, an R(116)-to-E mutation was introduced in the predicted sialic acid-binding domain of pSn, resulting in a mutant, pSn(RE), that could not bind sialic acids. PSn, but not pSn(RE), allowed PRRSV binding and internalization. These data show that the sialic acid-binding activity of pSn is essential for PRRSV attachment to pSn and thus identifies the variable, N-terminal domain of Sn as a PRRSV binding domain.

Indexed as

Virus AttachmentAmino Acid SubstitutionAnimalsBinding SitesCHO CellsCricetinaeCricetulusMacrophagesMembrane GlycoproteinsMutagenesis, Site-DirectedMutation, MissenseN-Acetylneuraminic AcidPorcine respiratory and reproductive syndrome virusProtein BindingProtein Structure, TertiaryReceptors, ImmunologicMembrane GlycoproteinsN-Acetylneuraminic AcidReceptors, ImmunologicReceptors, VirusSialic Acid Binding Ig-like Lectin 1

Identifiers

PMID17567703
PMCPMC1951444
OpenAlexW2054094621

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.