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Modeling of macromolecular proteins in prophenoloxidase cascade through experimental and computational approaches
Author(s) -
Sivakamavalli Jeyachandran,
Selvaraj Chandrabose,
Singh Sanjeev Kumar,
Vaseeharan Baskaralingam
Publication year - 2016
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1450
Subject(s) - prophenoloxidase , proteases , serine protease , biology , in silico , homology modeling , protease , innate immune system , protein structure , biochemistry , microbiology and biotechnology , immune system , computational biology , enzyme , genetics , gene
Prophenoloxidase (ProPO) cascade is a principal defense system in crustaceans, which consists of a variety of pattern recognition proteins (lipopolysaccharide and β‐glucan‐binding protein [β‐GBP], β‐GBP, and β‐glucan recognition protein), proteases (serine protease), and protease inhibitors (α2‐macroglobulin and pacifastin) to regulate the protection mechanism in crustaceans. In the prophneoloxidase pathway, the protein–protein interactions (PPIs) and other immune‐related analyses still have not been reported. Moreover, the structural features of ProPO cascade proteins have not yet been reported, hence we constructed the three‐dimensional structural features for all ProPO pathway proteins. Their PPIs were studied through an in silico approach. Laminarin has been identified as a triggering activator and it showed energetic binding with homology modeled β‐GBP and activated the β‐GBP, followed by the protein–protein complex formation leading to phenoloxidase synthesis. These findings provided a novel view of the ProPO mechanism and enhanced our knowledge of the innate immune system in crustaceans via computation. In conclusion, we propose a combined experimental and computational approach to analyze the mechanism of ProPO cascade proteins.