期刊
BIOMACROMOLECULES
卷 10, 期 7, 页码 1894-1903出版社
AMER CHEMICAL SOC
DOI: 10.1021/bm900300j
关键词
-
资金
- Ministry of Education, Science, Sports, and Culture of Japan [19310141, 18570135]
- Cooperation of Innovative Technology and Advanced Research in Evolutional Area
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan
- Grants-in-Aid for Scientific Research [18570135, 19310141] Funding Source: KAKEN
A series of spacer-N-linked glycopolymers carrying long/short alpha 2,3/6 sialylated glycan were designed as polymeric inhibitors of influenza virus. Lactose (Lac) and N-acetyllactosamine (LN: Gal beta 1,4GlcNAc) were first converted to spacer-N-linked disaccharide glycosides, followed by consecutive enzymatic addition of GlcNAc and Gal residues to the glycosides. The resulting spacer-N-linked glycosides with di-, tetra-, and hexasaccharides carrying a Lac, LN, lacto-N-neotetraose (LNnT: Gal beta 1,4GlcNAc beta 1,3Gal beta 1,4Glc), and LN beta 1,3LNnT were coupled to the carboxy group of gamma-polyglutamic acid (gamma-PGA) and enzymatically converted to glycopolypeptides carrying alpha 2,3/6 sialylated glycans. The interactions of a series of sialoglycopolypeptides with avian and human influenza virus strains were investigated using a hemagglutination inhibition assay. The avian virus A/Duck/HongKong/313/4/78 (H5N3) bound specifically, regardless of the structure of the asialo portion. In contrast, human virus A/Aichi/2/68 (H3N2) bound preferentially to long alpha 2,6sialylated glycans with penta- or heptasaccharides in a glycan length-dependent manner. Furthermore, the Sambucus sieboldiana (SNA) lectin was also useful as a model of human virus hemagglutinin (HA) for understanding the carbohydrate binding properties, because the recognition motifs of the inner sugar in the receptor were very similar.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据