Characterization of the Bovine Norovirus hemagglutinin
(English)Manuscript (preprint) (Other academic)
In this study we have analyzed the hemagglutination properties of bovine norovirus GIII.2 Newbury-2 virus like particles (VLPs). Hemagglutination (HA) and hemagglutination inhibition (HI) characteristics were investigated and results showed that bovine norovirus hemagglutinated bovine (6/8), pig (9/9) and rabbit (2/3) red blood cells (RBCs) but not RBC from goat, horse, guinea pig, sheep, chicken or humans. HA capacity differed between calfs and was temperature (4-22°C) and pH (4-10) independent. While three synthetic peptides constructed from the P-region of the capsid could not inhibit HA, a rabbit-peptide antiserum towards aa 365-379 inhibited HA. By homology modeling the bovine NoV shows a deletion close to the ligand binding site for Norwalk. This deletion may be responsible for the different binding patterns of the two strains. The peptide 365-379 was surface exposed and possibly located in a binding pocket. A set of 12 glycoconjugates including the proposed bovine receptor αGal1-3β1-4GlcNAc revealed that none could inhibit hemagglutination although αGal could bind the boVLPS. Neuraminidase did not affect HA suggesting that sialic acid is not a constituent of the HA receptor interaction. Trypsin-treatment of bovine RBCs increased HA titers and treatment with αgalactosidase of trypsin treated and non-trypsin treated RBCs eliminated HA activity suggesting that the αGal epitope is a potential receptor structure that might be connected to a glycolipid.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-68746OAI: oai:DiVA.org:liu-68746DiVA: diva2:420455