Cloning and functional analysis of the collectin gene from the grass carp Ctenopharyngodon idella.
- Author:
Qin LI
1
;
Meisheng MA
;
Chengyu HU
Author Information
1. Department of Bioscience, Nanchang University, Nanchang 330031, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Base Sequence;
Carps;
genetics;
Cloning, Molecular;
Collectins;
genetics;
physiology;
Fish Proteins;
genetics;
physiology;
Molecular Sequence Data;
Phylogeny;
Zebrafish;
genetics
- From:
Chinese Journal of Biotechnology
2010;26(1):22-27
- CountryChina
- Language:Chinese
-
Abstract:
The grass carp (Ctenopharyngodon idella) collectin gene was cloned from mixed liver and kidney cDNA library. The full length sequence of grass carp collectin was 1128 bp, contained a 5' untranslated region of 229 bp and a 3' untranslated region of 104 bp. The open reading frame of grass carp collectin was 795 bp which could code a 264 amino acids polypeptide, including a terminal codon. Phylogenetic analyses showed that grass carp collectin shared the highest homology with that of zebrafish (Danio rerio). To understand the function of grass carp collectin, we expressed and purified the recombinant protein (P(CRD)) that comprised carbohydrate recognition domain (CRD). Agglutination of Aeromonas hydrophila and Staphylococcus aureus etc. and sugars inhibition experiments showed that: galactose, glucose, mannose and maltose could inhibit the agglutination of Aeromonas hydrophila. Maltose could lower the agglutination of Staphylococcus aureus, whereas peptidoglycan and glucose inhibited it well. In addition, the activity of grass carp collectin could not dependent on Ca(2+).
