T160A mutation-induced deglycosylation at site 158 in hemagglutinin is a critical determinant of the dual receptor binding properties of clade 2.3. 4.4 H5NX subtype …
R Gao, M Gu, K Liu, Q Li, J Li, L Shi, X Li, X Wang… - Veterinary …, 2018 - Elsevier
Abstract Most clade 2.3. 4.4 H5NX subtype avian influenza viruses possess a T160A amino
acid substitution in the hemagglutinin (HA) protein that has been shown to affect the receptor
binding properties of a clade 2.3. 4 H5N1 virus. However, the effect of this single site
mutation on the HA backbone of clade 2.3. 4.4 H5NX viruses remains unclear. In this study,
two H5N6 field isolates possessing HA-160A with dual α-2, 3 and α-2, 6 receptor binding
properties (Y6 virus) and HA-160T with α-2, 3 receptor binding affinity (HX virus) …
acid substitution in the hemagglutinin (HA) protein that has been shown to affect the receptor
binding properties of a clade 2.3. 4 H5N1 virus. However, the effect of this single site
mutation on the HA backbone of clade 2.3. 4.4 H5NX viruses remains unclear. In this study,
two H5N6 field isolates possessing HA-160A with dual α-2, 3 and α-2, 6 receptor binding
properties (Y6 virus) and HA-160T with α-2, 3 receptor binding affinity (HX virus) …
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