JOURNAL ARTICLE

Diverse Sugar-Binding Specificities of Marine Invertebrate C-Type Lectins

Hiroki MatsubaraSachiko Nakamura‐TsurutaJun HirabayashiMitsuru JimboHisao KamiyaTomohisa OgawaKoji Muramoto

Year: 2007 Journal:   Bioscience Biotechnology and Biochemistry Vol: 71 (2)Pages: 513-519   Publisher: Oxford University Press

Abstract

The sugar-binding specificities of C-type lectins isolated from marine invertebrates were investigated by frontal affinity chromatography (FAC) using 100 oligosaccharides. The lectins included BRA-2 and BRA-3, multiple lectins from the hemolymph of the acorn barnacle, Megabalanus rosa, and BRL from the acorn barnacle, Balanus rostatus. The diverse sugar-binding specificities of the C-type lectins were determined by FAC analysis. BRA-2 recognized alpha2-6 sialylation but not alpha2-3 sialylation on glycans. On the other hand, BRA-3 showed high affinity for oligosaccharides with alpha-linked non-reducing terminal galactose, but not for sialylated forms, and BRL showed enhanced recognition activity towards Lewis(x) and Lewis(a) epitopes.

Keywords:
Hemolymph Barnacle Glycan Lectin Acorn Biochemistry Galactose Marine invertebrates Sugar Affinity chromatography Chemistry Balanus Biology Botany Crustacean Ecology Glycoprotein Enzyme

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Citation History

Topics

Invertebrate Immune Response Mechanisms
Life Sciences →  Immunology and Microbiology →  Immunology
Galectins and Cancer Biology
Life Sciences →  Immunology and Microbiology →  Immunology
Glycosylation and Glycoproteins Research
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology

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