Lectins CGL and MTL, representatives of mytilectin family, exhibit different antiproliferative activity in Burkitt's lymphoma cells.

Lectins are carbohydrate-binding proteins, whose biological effects are exerted via binding to glycoconjugates expressed on the surface of cells. Exposure to lectins can lead not only to a change in the structure and properties of cells but also to their death. Here, we studied the biological activity of lectins from the mussels Crenomytilus graynus (CGL) and Mytilus trossulus (MTL) and showed that these proteins can affect the proliferation of human lymphoma cells.

New l-Rhamnose-Binding Lectin from the Bivalve : Purification, Partial Structural Characterization and Antibacterial Activity.

In this study, a new l-rhamnose-binding lectin (GYL-R) from the hemolymph of bivalve was purified using affinity and ion-exchange chromatography and functionally characterized. Lectin antimicrobial activity was examined in different ways. The lectin was inhibited by saccharides possessing the same configuration of hydroxyl groups at C-2 and C-4, such as l-rhamnose, d-galactose, lactose, l-arabinose and raffinose.

Molecular Cloning and Characteristics of a Lectin from the Bivalve .

C-type lectins (CTLs) are a family of carbohydrate-binding proteins that mediate multiple biological events, including adhesion between cells, the turnover of serum glycoproteins, and innate immune system reactions to prospective invaders. Here, we describe the cDNA cloning of lectin from the bivalve (GYL), which encodes 161 amino acids and the C-type carbohydrate recognition domain (CRD) with EPN and WND motifs. The deduced amino acid sequence showed similarity to other CTLs.

Spatial Structure of Lectin from the Mussel : In-Sights from Molecular Modelling and Practical Proof.

Most proteins have the ability to self-associate into homooligomeric protein complexes, which consist of two or more identical subunits. Today, modern methods of molecular modeling are an integral part of the study of many biologically active molecules. In silico methods are widely used in structure establishing and function and activity prediction of lectins - carbohydrate-binding proteins.

Sulfated capsular polysaccharide from the marine bacterium Kangiella japonica inhibits T-47D cells growth in vitro.

Kangiella japonica KMM 3897 is a Gram-negative bacterium isolated from a coastal sea-water sample of the Sea of Japan. In this paper, the results about the structure and the antiproliferative effect on cancer cells of the capsular polysaccharide isolated from the Kangiella japonica KMM 3897 have been described. The carbohydrate polymer was isolated and purified by several separation techniques, and the structure was elucidated using chemical analysis and NMR spectroscopy.

Identification and Characterization of a Novel Lectin from the Clam and Its Functional Characterization under Microbial Stimulation and Environmental Stress.

Lectin from the bivalve (GYL) was purified by affinity chromatography on porcine stomach mucin-Sepharose. GYL is a dimeric protein with a molecular mass of 36 kDa, as established by SDS-PAGE and MALDI-TOF analysis, consisting of 18 kDa subunits linked by a disulfide bridge. According to circular dichroism data, GYL is a β/α-protein with the predominance of β-structure.

Structure and in vitro antiproliferative activity of the acidic capsular polysaccharide from the deep-sea bacterium Psychrobacter submarinus KMM 225.

Psychrobacter submarinus KMM 225 is a Gram-negative bacterium isolated from a sea-water sample collected at a depth of 300 m in the Northwest Pacific Ocean. Here we report the structure of the capsular polysaccharide from P. submarinus KMM 225 and its effect on the viability and colony formation of cancer cells.

Structure and in vitro Bioactivity against Cancer Cells of the Capsular Polysaccharide from the Marine Bacterium Psychrobacter .

Psychrobacter KMM 277 is a psychrophilic Gram-negative bacterium that has been isolated from the internal tissues of an ascidian sp. Here, we report the structure of the capsular polysaccharide from P. KMM 277 and its effect on the viability and colony formation of human acute promyelocytic leukemia HL-60 cells.

Structure of phosphorylated and sulfated polysaccharides from lipopolysaccharide of marine bacterium Marinicella litoralis KMM 3900.

Two polysaccharide fractions were obtained by mild acid degradation of the lipopolysaccharide of the marine bacterium Marinicella litoralis KMM 3900. The major polysaccharide was found to contain glycerol 1-phosphate (PGro) and methyl phosphate substituents (PMe), and the following structure of its disaccharide repeating unit was established by sugar analysis, dephosphorylation, Smith degradation, and 1D and 2D NMR spectroscopy: →4)-α-L-Rhap2PGro(~40%)-(1 → 3)-β-D-Manp6PMe(~80%)-(1 → . The minor polysaccharide was shown to consist of 4-O-sulfate-d-mannopyranosyl residues, non-stoichiometric methylated at O-3 and acetylated at O-6: →2)-α-D-Manp3R4S6Ac(~75%)-(1→, where R is Me (85%) or H (15%).

Structure and bioactivity of sulfated α-D-mannan from marine bacterium Halomonas halocynthiae KMM 1376.

Halomonas halocynthiae KMM 1376 is a Gram-negative bacterium that has been isolated from gill tissue of the ascidian Halocynthia aurantium. Mild acid hydrolysis of the lipopolysaccharide of H. halocynthiae KMM 1376 afforded an O-polysaccharide, which was studied by sugar analysis and NMR spectroscopy.

Structure, antiproliferative and cancer preventive properties of sulfated α-d-fucan from the marine bacterium Vadicella arenosi.

Sulfated fucose-containing glycopolymers are currently of great interest because of their wide spectrum of bioactivity, including anti-tumor properties. In this study, the structure of O-polysaccharide (OPS) of the marine bacterium Vadicella arenosi KMM 9024, its effect on the proliferation of human breast cancer MCF-7 cells and cancer preventive properties were investigated. Two OPS fractions with different molecular weights were isolated and purified from the lipopolysaccharide by mild acid hydrolysis followed by anion-exchange chromatography.

A GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus modulates immune response in macrophages and in mice.

A GalNAc/Gal-specific lectin (CGL) from the edible mussel Crenomytilus grayanus has been demonstrated to exhibit antibacterial properties. However, the mechanism of immune modulation by CGL in mammalian cells remains unclear. Here, we demonstrated that CGL can activate immune responses in macrophages and in mice.

А new Gal/GalNAc-specific lectin from the mussel Mytilus trossulus: Structure, tissue specificity, antimicrobial and antifungal activity.

In the present study, a new Gal/GalNAc specific lectin from the mussel Mytilus trossulus (designated as MTL) was identified, and its expression levels, both in tissues and toward pathogen stimulation, were then characterized. The MTL primary structure was determined via cDNA sequencing. Deduced sequence of 150 amino acid residues showed 89% similarity to lectins from the mussels Crenomytilus grayanus and Mytilus galloprovincialis that were the first members of a new family of zoolectins.

A lectin with antifungal activity from the mussel Crenomytilus grayanus.

Lectins (carbohydrate-binding proteins) are well known to actively participate in the defense functions of vertebrates and invertebrates where they play an important role in the recognition of foreign particles. In this study, we investigated of in vitro antifungal activity of lectin from the mussel Crenomytilus grayanus (CGL). Enzyme-linked immunosorbent assay indicated that CGL was predominantly detectable in tissues of mantle and to a lesser degree in the tissues of muscle, hepatopancreas, gill and hemocytes.

cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity.

An amino acid sequence of GalNAc/Gal-specific lectin from the mussel Crenomytilus grayanus (CGL) was determined by cDNA sequencing. CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectins family. According to circular dichroism results CGL is a β/α-protein with the predominance of β-structure.