| Literature DB >> 18203621 |
Peilin Zheng1, Hao Wang, Jianmin Zhao, Linsheng Song, Limei Qiu, Chaohua Dong, Bo Wang, Yunchao Gai, Changkao Mu, Chenghua Li, Duojiao Ni, Kezhi Xing.
Abstract
Lectins are a family of carbohydrate-recognition proteins which play crucial roles in innate immunity. In this study, a new lectin (CfLec-2) gene was cloned from Chlamys farreri by EST and RACE approaches. The full-length cDNA of CfLec-2 was composed of 708bp, encoding a typical long form carbohydrate-recognition domain of 130 residues. The deduced amino acid sequence showed high similarity to Brevican in Homo sapiens, C-type lectin-1 and lectin-2 in Anguilla japonica. The cDNA fragment encoding the mature peptide of CfLec-2 was recombined into plasmid pET-32a (+) and expressed in Escherichia coli Rosseta-Gami (DE3). The recombinant CfLec-2 (rCfLec-2) protein exhibited aggregative activity toward Staphylococcus haemolyticus, and the agglutination could be inhibited by d-mannose but not EDTA or d-galactose, indicating that CfLec-2 was a Ca2+ independent lectin. Moreover, rCfLec-2 could suppress the growth of E. coli TOP10F'. These results suggested that CfLec-2 was perhaps involved in the recognition and clearance of bacterial pathogens in scallop.Entities:
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Year: 2007 PMID： 18203621 DOI： 10.1016/j.fsi.2007.11.014
Source DB: PubMed Journal: Fish Shellfish Immunol ISSN： 1050-4648 Impact factor: 4.581