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

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...

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Bibliographic Details
Published in:Developmental and comparative immunology 2008, Vol.32 (5), p.487-499
Main Authors: Watanabe, Yasuharu, Shiina, Nobuyuki, Shinozaki, Fuminori, Yokoyama, Hiroshi, Kominami, Junko, Nakamura-Tsuruta, Sachiko, Hirabayashi, Jun, Sugahara, Kazuhiro, Kamiya, Hisao, Matsubara, Hiroki, Ogawa, Tomohisa, Muramoto, Koji
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Ayu
Brackish
Fish egg
Fish Proteins - chemistry
Fish Proteins - isolation & purification
Fish Proteins - metabolism
Freshwater
Gb3
Glugea plecoglossi
Glycolipid
Glycoprotein
Immunity, Innate
Lectin
Lectins - chemistry
Lectins - isolation & purification
Lectins - metabolism
Marine
Microsporidia - metabolism
Microsporidian
Molecular Sequence Data
Osmeriformes - immunology
Osmeriformes - parasitology
Ovum
Phylogeny
Plecoglossus altivelis
Rhamnose - metabolism
Rhamnose-binding lectin
Spores, Protozoan - metabolism
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Summary: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.
ISSN:0145-305X
1879-0089
DOI:10.1016/j.dci.2007.08.007