Human influenza virus recognition of sialyloligosaccharides.
Sialic acids are essential components of cell-surface receptors utilized by influenza viruses. To evaluate the recognition of asialic sugar parts of the receptor, three representative strains of human influenza A and B viruses were tested for their binding of a panel of sialyloligosaccharides. The highest affinity binding carbohydrate determinants recognized by the viruses in a context of different core structures were Neu5Ac alpha 2-3Gal for the type B virus, Neu5Ac alpha 2-6 Gal for the H3 subtype virus, and Neu5Ac alpha 2-6Gal beta 1-4GlcNAc for the H1 subtype virus. Penultimate to these determinants parts of the sialyloligosaccharides studied either contributed less significantly to the binding affinity, or interfered with the binding.
Gambaryan
A S
AS
M.P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region.
Piskarev
V E
VE
Yamskov
I A
IA
Sakharov
A M
AM
Tuzikov
A B
AB
Bovin
N V
NV
Nifant'ev
N E
NE
Matrosovich
M N
MN
D001665:Binding Sites; D002240:Carbohydrate Sequence; D006801:Humans; D066298:In Vitro Techniques; D009980:Influenza A virus / Q000737:chemistry / Q000378:metabolism*; D009981:Influenza B virus / Q000378:metabolism*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism
D009844:Oligosaccharides; D011991:Receptors, Virus; C016735:sialooligosaccharides