Evidence map›Paper›PMID 19578439›Full record

ArticlePLoS pathogens2009

The alphaGal epitope of the histo-blood group antigen family is a ligand for bovine norovirus Newbury2 expected to prevent cross-species transmission.

Maha Zakhour, Nathalie Ruvoën-Clouet, Annie Charpilienne, Brigitte Langpap, Didier Poncet, Thomas Peters, Nicolai Bovin, Jacques Le Pendu

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 88 citations in OpenAlex.

  1. Clinical and Epidemiological Features of Calicivirus Infections in Cattle.Animals : an open access journal from MDPI · 2026
    Review
  2. Article
  3. Review
  4. Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. A unique combination of glycoside hydrolases inThe Journal of biological chemistry · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Virus recognition of glycan receptors.Current opinion in virology · 2019
    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

8 authors at 5 institutions in 5 countries.

Maha ZakhourINSERM, U892, Université de Nantes, Institut de Biologie, Nantes, France.
Nathalie Ruvoën-Clouet
Annie Charpilienne
Brigitte Langpap
Didier Poncet
Thomas Peters
Nicolai Bovin
Jacques Le Pendu
Nantes Université · FRProteome Sciences (United Kingdom) · GBUniversity of Lübeck · DEInserm · FRInstitute of Bioorganic Chemistry · BY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among Caliciviridae, the norovirus genus encompasses enteric viruses that infect humans as well as several animal species, causing gastroenteritis. Porcine strains are classified together with human strains within genogroup II, whilst bovine norovirus strains represent genogroup III. Various GI and GII human strains bind to carbohydrates of the histo-blood group family which may be shared among mammalian species. Genetic relatedness of human and animal strains as well as the presence of potentially shared ligands raises the possibility of norovirus cross-species transmission. In the present study, we identified a carbohydrate ligand for the prototype bovine norovirus strain Bo/Newbury2/76/UK (NB2). Attachment of virus-like particles (VLPs) of the NB2 strain to bovine gut tissue sections showed a complete match with the staining by reagents recognizing the Galalpha1,3 motif. Alpha-galactosidase treatment confirmed involvement of a terminal alpha-linked galactose. Specific binding of VLPs to the alphaGal epitope (Galalpha3Galbeta4GlcNAcbeta-R) was observed. The binding of Galalpha3GalalphaOMe to rNB2 VLPs was characterized at atomic resolution employing saturation transfer difference (STD) NMR experiments. Transfection of human cells with an alpha1,3galactosyltransferase cDNA allowed binding of NB2 VLPs, whilst inversely, attachment to porcine vascular endothelial cells was lost when the cells originated from an alpha1,3galactosyltransferase KO animal. The alphaGal epitope is expressed in all mammalian species with the exception of the Hominidaea family due to the inactivation of the alpha1,3galactosyltransferase gene (GGTA1). Accordingly, the NB2 carbohydrate ligand is absent from human tissues. Although expressed on porcine vascular endothelial cells, we observed that unlike in cows, it is not present on gut epithelial cells, suggesting that neither man nor pig could be infected by the NB2 bovine strain.

Indexed as

ABO Blood-Group Systemalpha-GalactosidaseAnimalsAntigens, HeterophileCaliciviridae InfectionsCattleDuodenumEpitopesHemagglutinationHistocytochemistryIntestinal MucosaLigandsNorovirusNuclear Magnetic Resonance, BiomolecularOligosaccharidesSalivaABO Blood-Group Systemalpha-Galactosidasealpha-galactosyl epitopeAntigens, HeterophileEpitopesLigandsOligosaccharidesTrisaccharides

Identifiers

PMID19578439
PMCPMC2699481
OpenAlexW2094218250

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.