A galactose-binding lectin isolated from Aplysia kurodai (sea hare) eggs inhibits streptolysin-induced hemolysis.

A specific galactose-binding lectin was shown to inhibit the hemolytic effect of streptolysin O (SLO), an exotoxin produced by Streptococcus pyogenes. Commercially available lectins that recognize N-acetyllactosamine (ECA), T-antigen (PNA), and Tn-antigen (ABA) agglutinated rabbit erythrocytes, but had no effect on SLO-induced hemolysis. In contrast, SLO-induced hemolysis was inhibited by AKL, a lectin purified from sea hare (Aplysia kurodai) eggs that recognizes α-galactoside oligosaccharides.

Cytotoxicity and glycan-binding profile of a D-galactose-binding lectin from the eggs of a Japanese sea hare (Aplysia kurodai).

A divalent cation-independent 16 kDa D-galactose binding lectin (AKL-2) was isolated from eggs of sea hare, Aplysia kurodai. The lectin recognized D-galactose and D-galacturonic acid and had a 32 kDa dimer consisting of two disulfide-bonded 16 kDa subunits. Eighteen N-terminus amino acids were identified by Edman degradation, having unique primary structure.

A D-galactose-binding lectin purified from coronate moon turban, Turbo (Lunella) coreensis, with a unique amino acid sequence and the ability to recognize lacto-series glycosphingolipids.

A divalent, cation-independent d-galactose-binding lectin was purified from coronate moon turban Turbo (Lunella) coreensis. This lectin recognizes d-galactose and is a 38-kDa dimeric protein consisting disulphide-bonded 22-kDa polypeptides under non-reducing and reducing conditions of sodium dodecyl sulphate-polyacrylamide gel electrophoresis, respectively. Haemagglutination activity was inhibited by D-galactose, N-acetyl D-galactosamine, melibiose, lactose, porcine stomach mucin, asialofetuin and bovine submaxillary mucin.

Anti-fungal cell wall beta-glucan antibody in animal sera.

beta-Glucan is a major component of the cell walls and pathogen-associated microbial patterns of fungi. We previously reported the presence of an antibody which reacts to beta-glucan, anti-beta-glucan (BG) antibody, in human sera. In livestock and domestic pets, the antibody's response to fungal cell wall beta-glucan is little understood.

Isolation, purification, characterization and glycan-binding profile of a d-galactoside specific lectin from the marine sponge, Halichondria okadai.

A lectin recognizing both Galbeta1-3GlcNAc and Galbeta1-4GlcNAc was purified from the demosponge Halichondria okadai by lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 30 kDa by SDS-PAGE under reducing and non-reducing conditions and 60 kDa by gel permeation chromatography. The pI value of the lectin was 6.

[Isolation and serotyping of Vero toxin-producing Escherichia coli (VTEC) from pig].

As a part of basic studies to elucidate the source of infection of Verotoxin-producing Escherichia coli (VTEC) infectious disease, fresh feces were collected from pigs raised in Kanto District (A and B Prefectures) and Kyushu District (C and D Prefectures) between April and October in 2000, and isolation, serotyping, toxin typing, and drug sensitivity test of VTEC were performed. 1) Of 411 fecal samples tested, VTEC was isolated from 44 samples (10.7%), consisting of 12 of 112 samples (10.

[Identification of chemical structure of antibacterial components against Legionella pneumophila in a coffee beverage].

We previously reported that certain constituents in brewed coffee exhibited antibacterial activities against a strain of Legionella pneumophila. The constituents showing antibacterial activities were included only in extracts cold with water or hot water. To determine the antibacterial substances in coffee extract, the extract was fractionated by HPLC using a UV/photodiode array detector.