Back to Search
Start Over
Glycan-specificity of four neuraminidase-sensitive animal rotavirus strains
- Source :
- Veterinary microbiology. 207
- Publication Year :
- 2017
-
Abstract
- Group A rotaviruses (RVAs) are divided into neuraminidase (NA)-sensitive and NA-insensitive strains depending upon their binding affinity to the VP8* domain in the terminal sialic acids (SAs) of cell surface carbohydrates. Although NA-sensitive strains are known to use terminal SAs as an attachment factor, the exact nature of this attachment factor is largely unknown. Here we show that the specific linkage of SA-containing glycan to glycoprotein or glycolipid is an attachment factor used by NA-sensitive porcine G9P[7] PRG9121 and G9P[23] PRG942, bovine G6P[1] NCDV, and canine G3P[3] strains. Infectivity of porcine G9P[7] and G9P[23] strains was markedly blocked by α2,3-linkage and α2,6-linkage inhibitors, indicating that these strains bind to both α2,3- and α2,6-linked SAs. However, the infectivity of bovine G6P[1] and canine G3P[3] strains was significantly reduced by α2,6-linkage inhibitor but not by α2,3-linkage blockers, demonstrating a predilection of these strains for α2,6-linked SAs. The infectivity of four NA-sensitive strains was equally reduced by inhibitors of lipid membrane and N-linked glycoprotein but not by an inhibitor of O-linked glycoprotein, indicating that these strains utilize both glycolipid and N-linked glycoprotein. Our study demonstrates that four NA-sensitive animal strains could have a strain-dependent binding preference toward α2,6-linked SAs (P[1] NCDV and P[3] CU-1 strains) or both α2,3- and α2,6-linked SAs (P[7] PRG9121 and P[23] PRG942 strains) to the glycolipid and N-linked glycoprotein.
- Subjects :
- 0301 basic medicine
Rotavirus
Glycan
030106 microbiology
Cell
Neuraminidase
Virus Attachment
Biology
Sialidase
medicine.disease_cause
Microbiology
Cell Line
03 medical and health sciences
Glycolipid
medicine
Animals
Humans
chemistry.chemical_classification
Infectivity
Membrane Glycoproteins
General Veterinary
General Medicine
Fibroblasts
Molecular biology
030104 developmental biology
medicine.anatomical_structure
chemistry
biology.protein
Glycoprotein
Subjects
Details
- ISSN :
- 18732542
- Volume :
- 207
- Database :
- OpenAIRE
- Journal :
- Veterinary microbiology
- Accession number :
- edsair.doi.dedup.....469975910c437e06287baa46696f2f41