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Biotechnol Appl Biochem. 2015 May-Jun;62(3):416-23. doi: 10.1002/bab.1273. Epub 2014 Dec 1.

Molecular cloning, relative expression, and structural analysis of pattern recognition molecule β-glucan binding protein from mangrove crab Episesarma tetragonum.

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Department of Animal Health and Management, Crustacean Molecular Biology and Genomics Lab, Alagappa University, Karaikudi, Tamil Nadu, India.
Department of Bioinformatics, Computer Aided Drug Design and Molecular Modeling Lab, Alagappa University, Karaikudi, Tamil Nadu, India.


A full-length cDNA of a β-glucan binding protein (β-GBP) gene was identified from the mangrove crab Episesarma tetragonum. The open reading frame of the E. tetragonum β-GBP (Epte β-GBP) is 1,167 bp long, encoding a polypeptide of 389 amino acids. The deduced amino acid sequence of Epte β-GBP gene has conserved a potential recognition motif for β-1,3 linkages of polysaccharides and putative RGD (Arg-Gly-Asp) cell adhesion sites. Phylogenetic analysis of the Epte β-GBP gene showed the similarity with β-GBPs of other crustaceans and arthropods. Quantitative RT-PCR results showed the upregulation of Epte β-GBP gene expression in E. tetragonum hemocytes following a 12-H challenge in response to β-glucan (β-G). Epte β-GBP was involved in the regulation and activation of the prophenoloxidase cascade. A three-dimensional structure of active Epte β-GBP was modeled by homology modeling and refined with molecular dynamics simulations. A structural aspect of the protein is discussed based on experimental and theoretical results obtained.


RMSD; cloning; docking; molecular simulation; qRT-PCR; β-GBP

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