title: Interaction investigations of crustacean β-GBP recognition toward pathogenic microbial cell membrane and stimulate upon prophenoloxidase activation.
abstract: In invertebrates, crustaceans' immune system consists of pattern recognition receptors (PRRs) instead of immunoglobulin's, which involves in the microbial recognition and initiates the protein-ligand interaction between hosts and pathogens. In the present study, PRRs namely β-1,3 glucan binding protein (β-GBP) from mangrove crab Episesarma tetragonum and its interactions with the pathogens such as bacterial and fungal outer membrane proteins (OMP) were investigated through microbial aggregation and computational interaction studies. Molecular recognition and microbial aggregation results of Episesarma tetragonum β-GBP showed the specific binding affinity toward the fungal β-1,3 glucan molecule when compared to other bacterial ligands. Because of this microbial recognition, prophenoloxidase activity was enhanced and triggers the innate immunity inside the host animal. Our findings disclose the role of β-GBP in molecular recognition, host-pathogen interaction through microbial aggregation, and docking analysis. In vitro results were concurred with the in silico docking, and molecular dynamics simulation analysis. This study would be helpful to understand the molecular mechanism of β-GBP and update the current knowledge on the PRRs of crustaceans.
authors.affiliation: Crustacean Molecular Biology and Genomics Lab, Department of Animal Health and Management, Alagappa University, Karaikudi, 630 004, Tamil Nadu, India.
authors.forename: Jeyachandran
authors.initials: J
authors.lastname: Sivakamavalli
authors.forename: Chandrabose
authors.initials: C
authors.lastname: Selvaraj
authors.forename: Sanjeev Kumar
authors.initials: SK
authors.lastname: Singh
authors.forename: Baskaralingam
authors.initials: B
authors.lastname: Vaseeharan
mesh_terms: D000818:Animals; D001419:Bacteria / Q000276:immunology / Q000472:pathogenicity; D002352:Carrier Proteins / Q000235:genetics / Q000276:immunology; D004156:Catechol Oxidase / Q000235:genetics*; D002462:Cell Membrane / Q000201:enzymology / Q000276:immunology* / Q000382:microbiology; D003445:Crustacea / Q000276:immunology*; D004792:Enzyme Precursors / Q000235:genetics*; D054884:Host-Pathogen Interactions / Q000235:genetics / Q000276:immunology*; D007107:Immune System; D037102:Lectins / Q000235:genetics / Q000276:immunology; D051192:Receptors, Pattern Recognition / Q000235:genetics / Q000276:immunology
chemical_list: D002352:Carrier Proteins; D004792:Enzyme Precursors; D037102:Lectins; D051192:Receptors, Pattern Recognition; C037937:glucan-binding proteins; C038451:pro-phenoloxidase; D004156:Catechol Oxidase
keywords: CLSM; E. tetragonum; bacterial and fungal aggregation; biofilm inhibition; microbial aggregation; β-GBP; β-glucan