Substrate Specificity of Equine and Human Influenza A Virus Sialidase to Molecular Species of Sialic Acid

被引：5
|
作者：
Takahashi, Tadanobu [1 ,2 ]
Unuma, Saori [1 ,2 ]
Kawagishi, Sawako [1 ,2 ]
Kurebayashi, Yuuki [1 ,2 ]
Takano, Maiko [1 ,2 ]
Yoshino, Hiroki [1 ,2 ]
Minami, Akira [1 ,2 ]
Yamanaka, Takashi [3 ]
Otsubo, Tadamune [4 ]
Ikeda, Kiyoshi [4 ]
Suzuki, Takashi [1 ,2 ]
机构：
[1] Univ Shizuoka, Sch Pharmaceut Sci, Dept Biochem, 52-1 Yada, Shizuoka 4228526, Japan
[2] Global COE Program Innovat Human Hlth Sci, 52-1 Yada, Shizuoka 4228526, Japan
[3] Japan Racing Assoc, Equine Res Inst, Epizoot Res Ctr, 1400-4 Shiba, Shimotsuke, Tochigi 3290412, Japan
[4] Hiroshima Int Univ, Fac Pharmaceut Sci, Lab Synthet Organ Chem, 5-1-1 Hirokoshingai, Kure, Hiroshima 7370112, Japan
来源：
BIOLOGICAL & PHARMACEUTICAL BULLETIN | 2016年 / 39卷 / 10期
基金：
日本学术振兴会;
关键词：
equine influenza A virus; human influenza A virus; N-glycolyl neuraminic acid; Neu5Gc; neuraminidase; sialidase activity; N-GLYCOLYLNEURAMINIC ACID; NEURAMINIDASE; INFECTION; HEMAGGLUTININ; EPITHELIUM;
D O I：
10.1248/bpb.b16-00345
中图分类号：
R9 [药学];
学科分类号：
1007 ;
摘要：
Most equine influenza A viruses (IAVs) show strong binding to glycoconjugates containing N-glycolylneuraminic acid (Neu5Gc) as well as N-acetylneuraminic acid (Neu5Ac). Therefore, the progeny of equine IAV is thought to be released from the infected cell surface through removal of sialic acids by the viral sialidase. In the present study, equine IAV sialidases showed significantly lower substrate affinity than that of human IAV sialidases to artificial and natural Neu5Gc-conjugated substrates. The substrate specificity of equine IAV sialidases is in disagreement with their binding specificity to molecular species of sialic acid. The results suggest that substrate specificity of equine IAV sialidase for Neu5Ac, rather than for Neu5Gc, is important for an advantage at the early infection stage and the process of progeny virus release from the surface of infected cells.
引用
收藏
页码：1728 / 1733
页数：6
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