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

Yasuharu Watanabe, Nobuyuki Shiina, Fuminori Shinozaki, Hiroshi Yokoyama, Junko Kominami, Sachiko Nakamura-Tsuruta, Jun Hirabayashi, Kazuhiro Sugahara, Hisao Kamiya, Hiroki Matsubara, Tomohisa Ogawa, Koji Muramoto

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)487-499
Number of pages13
JournalDevelopmental and Comparative Immunology
Volume32
Issue number5
DOIs
Publication statusPublished - 2008

Keywords

  • Ayu
  • Fish egg
  • Gb3
  • Glugea plecoglossi
  • Glycolipid
  • Glycoprotein
  • Lectin
  • Microsporidian
  • Rhamnose-binding lectin

ASJC Scopus subject areas

  • Immunology
  • Developmental Biology

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