cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity
Overview of Kovalchuk SN et al.
| Authors | Kovalchuk SN Chikalovets IV Chernikov OV Molchanova VI Li W Rasskazov VA Lukyanov PA |
|---|---|
| Affiliation | G.B. Elyakov Pacific Institute of Bioorganic Chemistry Far Eastern Branch Russian Academy of Science Prospect 100 let Vladivostoku 159 Vladivostok 690022 Russian Federation. s.n.kovalchuk@gmail.com |
| Journal | Fish Shellfish Immunol |
| Year | 2013 |
Abstract
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. CGL was predicted to adopt a ß-trefoil fold. The lectin exhibits antibacterial activity and might be involved in the recognition and clearance of bacterial pathogens in the shellfish.