liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection
Univ Nantes, France.
Univ Nantes, France.
Univ Nantes, France; Univ Nantes, France.
Univ Nantes, France; Univ Nantes, France.
Show others and affiliations
2018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, article id 12961Article in journal (Refereed) Published
Abstract [en]

Human strains of rotavirus A (RVAs) recognize fucosylated glycans belonging to histo-blood group antigens (HBGAs) through their spike protein VP8*. Lack of these ligands due to genetic polymorphisms is associated with resistance to gastroenteritis caused by P[8] genotype RVAs. With the aim to delineate the contribution of HBGAs in the process, we analyzed the glycan specificity of VP8* proteins from various P genotypes. Binding to saliva of VP8* from P[8] and P[4] genotypes required expression of both FUT2 and FUT3 enzymes, whilst binding of VP8* from the P[14] genotype required FUT2 and A enzymes. We further defined a glycan motif, GlcNAc beta 3Gal beta 4GlcNAc, recognized by P[6] clinical strains. Conversion into Lewis antigens by the FUT3 enzyme impaired recognition, explaining their lower binding to saliva of Lewis positive phenotype. In addition, the presence of neutralizing antibodies was associated with the presence of the FUT2 wild type allele in sera from young healthy adults. Nonetheless, in vitro infection of transformed cell lines was independent of HBGAs expression, indicating that HBGAs are not human RV receptors. The match between results from saliva-based binding assays and the epidemiological data indicates that the polymorphism of human HBGAs controls susceptibility to RVAs, although the exact mechanism remains unclear.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2018. Vol. 8, article id 12961
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:liu:diva-151201DOI: 10.1038/s41598-018-31005-4ISI: 000442917500033PubMedID: 30154494OAI: oai:DiVA.org:liu-151201DiVA, id: diva2:1248042
Note

Funding Agencies|Agence Nationale de la Recherche (France): GASTROVIM; Region des Pays de la Loire (France): ARMINA; Merieux Research Grant GOMMs; Russian Science Foundation [14-5-00131]; Swedish Research Council [320301]

Available from: 2018-09-13 Created: 2018-09-13 Last updated: 2018-10-15

Open Access in DiVA

fulltext(2678 kB)56 downloads
File information
File name FULLTEXT01.pdfFile size 2678 kBChecksum SHA-512
d29847b358348cfeab3ba2c4c40f93ac59717a59fd5903b2df505ba95d155ecbdeadf593a7c10eb14d0a88c71b140b5f9eb62da3fb26ea5263658c46445f9dfa
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Nordgren, JohanSvensson, Lennart
By organisation
Division of Microbiology and Molecular MedicineFaculty of Medicine and Health Sciences
In the same journal
Scientific Reports
Microbiology in the medical area

Search outside of DiVA

GoogleGoogle Scholar
Total: 56 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 102 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf