title: Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6'-sialyl(N-acetyllactosamine).
abstract: Synthetic sialylglycoconjugates bearing 3'-sialyllactose, 6'-sialyllactose, or 6'-sialyl(N-acetyllactosamine) moieties attached to the polyacrylic acid carrier (P-3-SL, P-6-SL, and P-6-SLN, respectively) were prepared and tested for their ability to bind to influenza virus isolates from different hosts in a competitive solid phase assay. The virus panel included egg-grown avian and porcine strains, as well as human viruses isolated and propagated solely in mammalian (MDCK) cells and their egg-adapted variants. A clear correlation was observed between the pattern of virus binding of two glycopolymers, P-3-SL and P-6-SLN, and the host species from which the virus was derived. Avian isolates displayed a high binding affinity for P-3-SL and a two to three orders of magnitude lower affinity for P-6-SLN. By contrast, all non-egg-adapted human A and B viruses bound P-6-SLN strongly but did not bind P-3-SL. Unlike the "authentic" human strains, their egg-adapted counterparts acquired an ability to bind P-3-SL, indicative of a shift in the receptor-binding phenotype toward the recognition of Neu5Ac2-3Gal-terminated sugar sequences. Among the porcine viruses and human isolates with porcine hemagglutinin, few displayed an avian-like binding phenotype, while others differed from both avian and human strains by a reduced ability to discriminate between P-3-SL and P-6-SLN. Our data show that sialylglycopolymers may become a useful tool in studies on molecular mechanisms of interspecies transfer, tissue specificity, and other structure-function relationships of the influenza virus hemagglutinin.
authors.affiliation: M. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Moscow, Russia.
authors.forename: A S
authors.initials: AS
authors.lastname: Gambaryan
authors.forename: A B
authors.initials: AB
authors.lastname: Tuzikov
authors.forename: V E
authors.initials: VE
authors.lastname: Piskarev
authors.forename: S S
authors.initials: SS
authors.lastname: Yamnikova
authors.forename: D K
authors.initials: DK
authors.lastname: Lvov
authors.forename: J S
authors.initials: JS
authors.lastname: Robertson
authors.forename: N V
authors.initials: NV
authors.lastname: Bovin
authors.forename: M N
authors.initials: MN
authors.lastname: Matrosovich
mesh_terms: D000606:Amino Sugars / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D002642:Chick Embryo; D004285:Dogs; D006001:Glycoconjugates / Q000378:metabolism; D006801:Humans; D009980:Influenza A virus / Q000302:isolation & purification / Q000378:metabolism*; D009981:Influenza B virus / Q000302:isolation & purification / Q000378:metabolism*; D007785:Lactose / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D010641:Phenotype; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D012794:Sialic Acids / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000606:Amino Sugars; D006001:Glycoconjugates; D011991:Receptors, Virus; D012794:Sialic Acids; C032269:sialyl-N-acetyllactosamine; C000020:N-acetylneuraminoyllactose; D007785:Lactose