Isolation and characterization of l-rhamnose-binding lectin, which binds to microsporidian Glugea plecoglossi, from ayu (Plecoglossus altivelis) eggs

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• 作者：Yasuharu Watanabe ; Nobuyuki Shiina ; Fuminori Shinozaki ; Hiroshi Yokoyama ; Junko Kominami ; Sachiko Nakamura-Tsuruta ; Jun Hirabayashi ; Kazuhiro Sugahara ; Hisao Kamiya ; Hiroki Matsubara ; Tomohisa Ogawa
• 关键词：Ayu ; Fish egg ; Gb3 ; Glugea plecoglossi ; Glycolipid ; Glycoprotein ; Lectin ; Microsporidian ; Rhamnose-binding lectin
• 刊名：Developmental and Comparative Immunology
• 出版年：2008
• 出版时间：2008
• 年：2008
• 卷：32
• 期：5
• 页码：487-499
• 全文大小：1585 K

文摘

A rhamnose-binding lectin, named SFL, was isolated from the eggs of ayu (sweet fish, Plecoglossus altivelis) by affinity and ion-exchange chromatographies. SFL revealed 287 amino acid residues with 3 tandemly repeated domains, and contained 8 half-Cys residues in each domain. The lectin was shown to have a highly specific binding affinity to globotriaosylceramide (Gb3) by frontal affinity chromatography using 100 oligosaccharides. SFL was localized in several tissues and serum of both male and female ayu, such as gill, liver, ovary, testis, intestine, stomach, brain, kidney and serum. The lectin agglutinated the spores of the microsporidian Glugea plecoglossi, which is a pathogen of ayu. Although SFL bound to glycoproteins and glycolipids of G. plecoglossi spores, Gb3 could not be detected in either of them. The results suggest that SFL could interact with various glycoconjugates of pathogens to play a role in the adhesion of microorganisms invading in the body.