Title of article :
cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity
Author/Authors :
Kovalchuk، نويسنده , , Svetlana N. and Chikalovets، نويسنده , , Irina V. and Chernikov، نويسنده , , Oleg V. and Molchanova، نويسنده , , Valentina I. and Li، نويسنده , , Wei and Rasskazov، نويسنده , , Valery A. and Lukyanov، نويسنده , , Pavel A.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 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.
Keywords :
Crenomytilus grayanus , amino acid sequence , Antibacterial activity , GalNAc/Gal-specific lectin , ك-trefoil fold
Journal title :
Fish and Shellfish Immunology
Journal title :
Fish and Shellfish Immunology
