Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.18 extracted from

  • Shtyrya, Y.; Mochalova, L.; Voznova, G.; Rudneva, I.; Shilov, A.; Kaverin, N.; Bovin, N.
    Adjustment of receptor-binding and neuraminidase substrate specificities in avian-human reassortant influenza viruses (2009), Glycoconj. J., 26, 99-109.
    View publication on PubMed

Application

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

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

Organism UniProt Comment Textmining
unidentified influenza virus
-
-
-