Characterization of multisugar-binding C-type lectin (SpliLec) from a bacterial-challenged cotton leafworm, Spodoptera littoralis.

ABSTRACT:

Background

Various proteins that display carbohydrate-binding activity in a Ca(2+)-dependent manner are classified into the C-type lectin family. They have one or two C-type carbohydrate-recognition domains (CRDs) composed of 110-130 amino acid residues in common. C-type lectins mediate cell adhesion, non-self recognition, and immuno-protection processes in immune responses and thus play significant roles in clearance of invaders, either as cell surface receptors for microbial carbohydrates or as soluble proteins existing in tissue fluids. The lectin of Spodoptera littoralis is still uncharacterized.

Methodology

A single orf encoding a deduced polypeptide consisting of an 18-residue signal peptide and a 291-residue mature peptide, termed SpliLec, was isolated from the haemol

SUBMITTER: Seufi AM 

PROVIDER: S-EPMC3423437 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature