Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai

• Published in: Toxins 2012-05, Vol.4 (5), p.323-338
• Main Authors: Matsumoto, Ryo, Fujii, Yuki, Kawsar, Sarkar M A, Kanaly, Robert A, Yasumitsu, Hidetaro, Koide, Yasuhiro, Hasan, Imtiaj, Iwahara, Chihiro, Ogawa, Yukiko, Im, Chang Hun, Sugawara, Shigeki, Hosono, Masahiro, Nitta, Kazuo, Hamako, Jiharu, Matsui, Taei, Ozeki, Yasuhiro
• Format: Article
• Language: English
• Subjects: Animals; Cell Survival - drug effects; Cytotoxicity; Cytotoxins - metabolism; Cytotoxins - pharmacology; Hemagglutination Tests; Hexosamines; Humans; Jurkat Cells; K562 Cells; Lectins - isolation & purification; Lectins - metabolism; Lectins - pharmacology; Leukemia; Mucins; Polysaccharides - metabolism; Porifera
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins4050323

A divalent cation-independent lectin-HOL-18, with cytotoxic activity against leukemia cells, was purified from a demosponge, Halichondria okadai. HOL-18 is a 72 kDa tetrameric lectin that consists of four non-covalently bonded 18 kDa subunits. Hemagglutination activity of the lectin was strongly inhibited by chitotriose (GlcNAcβ1-4GlcNAcβ1-4GlcNAc), fetuin and mucins from porcine stomach and bovine submaxillary gland. Lectin activity was stable at pH 4-12 and temperatures lower than 60 °C. Frontal affinity chromatography with 16 types of pyridylaminated oligosaccharides indicated that the lectin had an affinity for N-linked complex-type and sphingolipid-type oligosaccharides with N-acetylated hexosamines and neuramic acid at the non-reducing termini. The lectin killed Jurkat leukemia T cells and K562 erythroleukemia cells in a dose- and carbohydrate-dependent manner.