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

被引：8

作者：

Ogata, Makoto ^{[1
]}

Koizumi, Ami ^{[1
]}

Otsubo, Tadamune ^{[2
]}

Ikeda, Kiyoshi ^{[2
]}

Sakamoto, Mao ^{[1
]}

Aita, Rena ^{[1
]}

Kato, Tatsuya ^{[3
]}

Park, Enoch Y. ^{[3
]}

Yamanaka, Takashi ^{[4
]}

Hidari, Kazuya I. P. J. ^{[5
]}

机构：

[1] Fukushima Coll, Natl Inst Technol, Dept Chem & Biochem, Iwaki, Fukushima, Japan

[2] Hiroshima Int Univ, Sch Pharmaceut Sci, Dept Organ Chem, Kure, Japan

[3] Shizuoka Univ, Res Inst Green Sci & Technol, Suruga Ku, Shizuoka, Japan

[4] Japan Racing Assoc, Equine Res Inst, Epizoot Res Ctr, Shimotsuke, Tochigi, Japan

[5] Univ Aizu, Jr Coll Div, Dept Food & Nutr, Yahata, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2017年 / 81卷 / 08期

关键词：

cluster effect; glycopolymer; influenza virus; interspecies transmission; sialic acid; SIALIC-ACID; A VIRUSES; MULTIVALENT SIALYLOLIGOSACCHARIDES; INFECTION; RECEPTOR; GLYCOPOLYMERS; MEMBRANE; BACKBONE; BINDING; DESIGN;

D O I：

10.1080/09168451.2017.1325315

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A series of novel sialoglycopolypeptides carrying N-glycolylneuraminic acid (Neu5Gc)-containing trisaccharides having alpha(2 -> 3)-and alpha(2 -> 6)-linkages in the side chains of.-polyglutamic acid (gamma-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 alpha 2,3-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.

引用

页码：1520 / 1528

页数：9

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[21] Improved expression of fusion protein using a cysteine-protease- and chitinase-deficient Bombyx mori (silkworm) multiple nucleopolyhedrovirus bacmid in silkworm larvae [J].