[Reduction of the functional match of influenza virus hemagglutinin and neuraminidase after reassortation of genes].
Influenza virus A (FluA) reassortants with low-functional neuraminidase (NA) of subtype N1 and hemagglutinin (HA) of subtypes H2, H3, H4, and H13 display virion aggregation and accumulate to a lower titer because sialyl residues are not completely removed from virion components. Nonaggregating variants of FluA (H13N1) were shown to result from a mutation that reduces the HA affinity for sialyl substrates. Amino acid substitution K156E, which increases a negative charge at the edge of the receptor-binding pocket of HA large subunit (HA1), was revealed in two independent variants. This substitution was the only difference between HA1 of the original reassortant and one of its variants and, therefore, accounted for restoration of the functional match between HA and NA.
Rudneva
I A
IA
Gambarian
A S
AS
Shilov
A A
AA
Sinitsyn
B V
BV
Kropotkina
E A
EA
Il'iushina
N A
NA
Kaverin
N V
NV
D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism*; D009980:Influenza A virus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D009439:Neuraminidase / Q000378:metabolism*; D016865:Reassortant Viruses / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D009439:Neuraminidase