Molecular cloning, sequence characterization, and expression analysis of C-type lectin (CTL) and ER-Golgi intermediate compartment 53-kDa protein (ERGIC-53) homologs from the freshwater prawn, Macrobrachium rosenbergii
- Authors
- Baliarsingh, Snigdha; Sahoo, Sonalina; Jo, Yong Hun; Han, Yeon Soo; Sarkar, Arup; Lee, Yong Seok; Mohanty, Jyotirmaya; Patnaik, Bharat Bhusan
- Issue Date
- Apr-2022
- Publisher
- Kluwer Academic Publishers
- Keywords
- Macrobrachium rosenbergii; CTL; ERGIC-53; Immune response; V. harveyi
- Citation
- Aquaculture International, v.30, no.2, pp 1011 - 1035
- Pages
- 25
- Journal Title
- Aquaculture International
- Volume
- 30
- Number
- 2
- Start Page
- 1011
- End Page
- 1035
- URI
- https://scholarworks.bwise.kr/sch/handle/2021.sw.sch/20658
- DOI
- 10.1007/s10499-022-00845-3
- ISSN
- 0967-6120
1573-143X
- Abstract
- Lectin protein families are diverse and multi-functional in crustaceans. The carbohydrate-binding domains (CRDs) of lectins recognize the molecular patterns associated with pathogens and orchestrate important roles in crustacean defense. In this study, two lectin homologs, a single CRD containing C-type lectin (CTL) and an L-type lectin (LTL) domain containing endoplasmic reticulum Golgi intermediate compartment 53 kDa protein (ERGIC-53) were identified from the freshwater prawn, Macrobrachium rosenbergii. The open reading frames of MrCTL and MrERGIC-53 were 654 and 1,515 bp, encoding polypeptides of 217 and 504 amino acids, respectively. Further, MrCTL showed a 20-amino acid transmembrane helix region and 10 carbohydrate-binding residues within the CRD. MrERGIC-53 showed a signal peptide region, a type-I transmembrane region, and a coiledcoil region at the C-terminus. Phylogenetic analysis revealed a close relationship between MrCTL and MrLectin and M. nipponense CTL (MnCTL), whereas MrERGIC-53 shared high sequence identity with Eriocheir sinensis ERGIC-53 and Penaeus vannamei MBL-1. A homology-based model predicted small carbohydrate-combining sites with a metal-binding site for ligand binding (Ca2+ binding site) in MrCTL and beta-sheets connected by short loops and beta-bends forming a dome-shaped beta-barrel structure representing the LTL domain of MrERGIC-53. Quantitative real-time polymerase chain reaction detected MrCTL and MrERGIC-53 transcripts in all examined tissues, with particularly high levels observed in hemocytes, hepatopancreas, and mucosal-associated tissues, such as the stomach and intestine. Further, the expression levels of MrCTL and MrERGIC-53 transcripts were remarkably altered after V. harveyi challenge, suggesting putative function in host innate immunity.
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