Cloning and characterization of two different L-type lectin genes from the Chinese mitten crab Eriocheir sinensis
Developmental & Comparative Immunology, ISSN: 0145-305X, Vol: 46, Issue: 2, Page: 255-266
2014
- 26Citations
- 23Captures
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Metrics Details
- Citations26
- Citation Indexes26
- 26
- CrossRef15
- Captures23
- Readers23
- 23
Article Description
L-type lectins contain a leguminous lectin domain and bind to high-mannose type oligosaccharides. In the secretory pathway, L-type lectins play crucial functions in the trafficking, sorting, and targeting of maturing glycoproteins. This study identified two novel L-type lectins, designated as EsERGIC-53 and EsVIP36, from the Chinese mitten crab Eriocheir sinensis. The complete nucleotide sequence of ERGIC-53 cDNA was 1955 bp, containing a 1506 bp open reading frame (ORF) encoding a putative protein of 501 deduced amino acids. The full-length cDNA of VIP36 was 3474 bp with a 984 bp ORF encoding a 327-amino acid peptide. The deduced ERGIC-53 and VIP36 proteins contained a putative signal peptide and an L-type lectin-like domain. Phylogenetic analysis showed that ERGIC-53 and VIP36 belonged to different clades of L-type lectin family. Reverse transcription PCR showed that ERGIC-53 and VIP36 were expressed in all tested tissues. Quantitative real-time RT-PCR analysis revealed that ERGIC-53 and VIP36 transcripts in hepatopancreas were significantly induced at various time points after infection with lipopolysaccharide (LPS), peptidoglycan (PGN), Staphylococcus aureus, Vibrio parahaemolyticus, and Aeromonas hydrophila. A bacterium-binding experiment showed that both ERGIC-53 and VIP36 could bind to different microbes. Sugar binding assay revealed that these lectins could also bind to the glycoconjugates of bacteria surface, such as LPS, PGN, d -Mannose, and N-Acetyl- d -mannosamine. Moreover, these two L-type lectins agglutinated bacteria in a calcium-dependent manner, and both exerted the ability of facilitating the clearance of injected bacteria V. parahaemolyticus in the crab. Our results suggested that ERGIC-53 and VIP36 functioned as pattern recognition receptors in the immune system of E. sinensis.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0145305X14001207; http://dx.doi.org/10.1016/j.dci.2014.04.015; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84901324368&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/24796868; https://linkinghub.elsevier.com/retrieve/pii/S0145305X14001207; https://dx.doi.org/10.1016/j.dci.2014.04.015
Elsevier BV
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