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Molecular characterization and expression analysis of Lily-type lectin (SmLTL) in turbot Scophthalmus maximus, and its response to Vibrio anguillarum

A full-length lily-type lectin ( Sm LTL) was identified from turbot ( Scophthalmus maximus ) in this study. By searching database for protein identification and function prediction, Sm LTL were confirmed. The full-length cDNA of Sm LTL is composed of 569 bp and contains a 339 bp ORF that encodes 112...

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Published in:Journal of oceanology and limnology 2018-03, Vol.36 (2), p.508-518
Main Authors: Xia, Dandan, Ma, Aijun, Huang, Zhihui, Shang, Xiaomei, Cui, Wenxiao, Yang, Zhi, Qu, Jiangbo
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description A full-length lily-type lectin ( Sm LTL) was identified from turbot ( Scophthalmus maximus ) in this study. By searching database for protein identification and function prediction, Sm LTL were confirmed. The full-length cDNA of Sm LTL is composed of 569 bp and contains a 339 bp ORF that encodes 112 amino acid residues. The Sm LTL peptide is characterized by a specific β-prism architecture and contains three mannose binding sites in a three-fold internal repeat between amino acids 30–99; two of the repeats share the classical mannose binding domain (QxDxNxVxY) while the third binding site was similar to other fish-specific binding motifs (TxTxGxRxV). The primary, secondary, and tertiary structures of Sm LTL were predicted and analyzed, indicating that the Sm LTL protein was hydrophilic, contained 5.36% α-helices, 39.29% extended strands, 16.07% β-folds, and 39.29% random coils, and three β-folds. Quantitative realtime polymerase chain reaction (qPCR) analysis revealed that the Sm LTL mRNA was abundantly expressed in skin, gill, and intestine. Low levels of Sm LTL expression were observed in other tissues. The expression of Sm LTL in gill, skin and intestine increased at mRNA level after stimulation of Vibrio anguillarum, our results suggest that Sm LTL serve as the first line of defence against microbial infections and play a pivotal role in the innate mucosal immune system. The current study indicates that Sm LTL is a member of the lilytype lectin family and the information reported here will provide an important foundation for future research on the role of this protein.
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subjects Amino acids
Bacteria
Binding sites
Biology
Complementary DNA
Earth and Environmental Science
Earth Sciences
Fish
Helices
Immune system
Immunity
Intestine
Intestines
Lectins
Mannose
Marine fishes
Microorganisms
mRNA
Mucosal immunity
Nucleotide sequence
Oceanography
Open reading frames
PCR
Polymerase chain reaction
Proteins
Scophthalmus maximus
Tertiary
Vibrio anguillarum
title Molecular characterization and expression analysis of Lily-type lectin (SmLTL) in turbot Scophthalmus maximus, and its response to Vibrio anguillarum
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