Application | Comment | Organism |
---|---|---|
medicine | study on functional compatibility of hemagglutinin and neuraminidase on the oligosaccharide level, through measuring the receptor-binding and substrate specificities of reassortant/passage human-avian variant virus pairs. Selection of the high-yield variants of the human-avian reassortants leads either to twofold decrease in the affinity of HA for most alpha2-3-sialosides and the appearance of affinity for alpha2-6-sialosides like in the H3N2 reassortant, or to decreasing the hemagglutinin affinity for Neu5Acalpha2-3Galbeta1-3GlcNAc and Neu5Acalpha2-3Galbeta1-3(Fucalpha1-4)GlcNAc in the H3N1 reassortant, or to enhancing the ability of neuraminidase to discriminate between alpha2-3/2-6 substrates in the H4N1 reassortant | unidentified influenza virus |
Protein Variants | Comment | Organism |
---|---|---|
D79V/S366N | mutation isolated in influenza virus subtype H3N1 | unidentified influenza virus |
E83G | mutation isolated in influenza virus subtype H3N2 | unidentified influenza virus |
L206I | mutation isolated in influenza virus subtype H4N1 | unidentified influenza virus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
unidentified influenza virus | - |
- |
- |