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

Authors :: Kovalchuk SN
Chikalovets IV
Chernikov OV
Molchanova VI
Li W
Rasskazov VA
Lukyanov PA
Source :: Fish & shellfish immunology [Fish Shellfish Immunol] 2013 Oct; Vol. 35 (4), pp. 1320-4. Date of Electronic Publication: 2013 Jul 22.
Publication 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.<br /> (Copyright © 2013 Elsevier Ltd. All rights reserved.)

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