cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity.
Fish Shellfish Immunol
; 35(4): 1320-4, 2013 Oct.
Article
em En
| MEDLINE
| ID: mdl-23886951
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 ß/α-protein with the predominance of ß-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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Mytilidae
/
Lectinas
Limite:
Animals
Idioma:
En
Revista:
Fish Shellfish Immunol
Assunto da revista:
BIOLOGIA
/
MEDICINA VETERINARIA
Ano de publicação:
2013
Tipo de documento:
Article