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Mol Immunol. 2013 Dec;56(4):497-506. doi: 10.1016/j.molimm.2013.06.020. Epub 2013 Aug 1.

Fish lily type lectin-1 contains β-prism architecture: immunological characterization.

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Division of Fisheries Biotechnology & Molecular Biology, Department of Biotechnology, Faculty of Science and Humanities, SRM University, Kattankulathur 603 203, Chennai, Tamil Nadu, India; Department of Microbiology, SRM Arts & Science College, Kattankulathur 603 203, Chennai, India.


In this study we report a full-length lily type lectin-1 (CsLTL-1) identified from striped murrel, Channa striatus. CsLTL-1 was identified from the established C. striatus cDNA library using GS-FLX™ genome sequencing technology and was found to contain 354 nucleotide base pairs and its open reading frame (ORF) encodes a 118 amino acid residue. CsLTL-1 mRNA is predominately expressed in the gills and is up-regulated upon infection with fungus (Aphanomyces invadans) and bacteria (Aeromonas hydrophila). Hemagglutination studies with recombinant CsLTL-1 show that, at 4μg/ml agglutinates occurs in a calcium independent manner and is inhibited in the presence of d-mannose (50mM) and d-glucose (100mM). The CsLTL-1 sequence was completely characterized using various bioinformatics tools. CsLTL-1 peptide contains a mannose binding site at 30-99 along with its specific motif of β-prism architecture. The phylogenetic analysis showed that CsLTL-1 clustered together with LTL-1 from Oplegnathus fasciatus. CsLTL-1 protein 3D structure was predicted by I-Tasser program and the model was evaluated using Ramachanran plot analysis. The secondary structure analysis of CsLTL-1 reveals that the protein contains 23% β-sheets and 77% coils. The overall results showed that CsLTL-1 is an important immune gene involved in the recognition and elimination of pathogens in murrels.


Channa striatus; Gene expression; Hemagglutination assay; Lily type lectin; Sugar binding specificity

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