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Biosci Biotechnol Biochem. 2017 Aug;81(8):1520-1528. doi: 10.1080/09168451.2017.1325315. Epub 2017 May 18.

Chemoenzymatic synthesis and characterization of N-glycolylneuraminic acid-carrying sialoglycopolypeptides as effective inhibitors against equine influenza virus hemagglutination.

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a Department of Chemistry and Biochemistry, National Institute of Technology , Fukushima College , Iwaki , Japan.
b Department of Organic Chemistry , School of Pharmaceutical Sciences, Hiroshima International University , Kure-shi , Japan.
c Research Institute of Green science and Technology , Shizuoka University , Suruga-ku , Japan.
d Epizootic Research Center, Equine Research Institute , Japan Racing Association , Tochigi , Japan.
e Department of Food and Nutrition, Junior College Division , University of Aizu , Yahata , Japan.


A series of novel sialoglycopolypeptides carrying N-glycolylneuraminic acid (Neu5Gc)-containing trisaccharides having α(2 → 3)- and α(2 → 6)-linkages in the side chains of γ-polyglutamic acid (γ-PGA) were designed as competitive inhibitors against equine influenza viruses (EIV), which critically recognize the Neu5Gc residue for receptor binding. Using horse red blood cells (HRBC) we successfully evaluated the binding activity of the multivalent Neu5Gc ligands to both equine and canine influenza viruses in the hemagglutination inhibition (HI) assay. Our findings show the multivalent α2,3-linked Neu5Gc-ligands (3a-c and 7) selectively inhibit hemagglutination mediated by both influenza viruses and display a strong inhibitory activity. Our results indicate that the multivalent Neu5Gc-ligands can be used as novel probes to elucidate the mechanism of infection/adhesion of Neu5Gc-binding influenza viruses.


cluster effect; glycopolymer; influenza virus; interspecies transmission; sialic acid

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