alpha-Neup5Ac-(2--3)-beta-D-Galp-(1--4)-[alpha-L-Fucp-(1--3)]-D-GlcpNAc has been researched along with Orthomyxoviridae-Infections* in 1 studies
1 other study(ies) available for alpha-Neup5Ac-(2--3)-beta-D-Galp-(1--4)-[alpha-L-Fucp-(1--3)]-D-GlcpNAc and Orthomyxoviridae-Infections
| Article | Year |
|---|---|
Mutation W222L at the Receptor Binding Site of Hemagglutinin Could Facilitate Viral Adaption from Equine Influenza A(H3N8) Virus to Dogs.
An outbreak of respiratory disease caused by the equine-origin influenza A(H3N8) virus was first detected in dogs in 2004 and since then has been enzootic among dogs. Currently, the molecular mechanisms underlying host adaption of this virus from horses to dogs is unknown. Here, we have applied quantitative binding, growth kinetics, and immunofluorescence analyses to elucidate these mechanisms. Our findings suggest that a substitution of W222L in the hemagglutinin of the equine-origin A(H3N8) virus facilitated its host adaption to dogs. This mutation increased binding avidity of the virus specifically to receptor glycans with Topics: Animals; Binding Sites; Dogs; Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins; Horses; Host Specificity; Influenza A Virus, H3N8 Subtype; Kinetics; Mutation; Neuraminic Acids; Oligosaccharides; Orthomyxoviridae Infections; Protein Binding; Receptors, Virus; Sialyl Lewis X Antigen; Trachea; Viral Tropism; Virus Attachment | 2018 |