Abstract
Clostridium perfringens beta-toxin (CPB) is linked to necrotic enteritis (over proliferation of bacteria) in several species showing cytotoxic effect on primary porcine endothelial and human precursor immune cells. P2X7 receptor on THP-1 cells is known to bind CPB. This is critical to understand the mechanism of pore formation for effective drug design. The structure of CPB and P2X7 receptor proteins were modeled using standard molecular modeling procedures (I-TASSER and Robetta server). This is followed by protein-protein docking (HADDOCK server) to study their molecular interaction. Interacting residues (19 residues from CPB and 21 residues from P2X7) were identified using the PISA server. Thus, we document the molecular docking analysis of P2X7 receptor with the beta toxin from Clostridium perfringens towards drug design and development of drugs to control necrotic enteritis.
Highlights
C. perfringens type C strain causes lethal infections such as necrotic enteritis and enterotoxaemia in small bowel of cattle, sheep, goats and humans
It has been reported that alpha-toxin from S. aureus induced its cytotoxic effects through P2X7 receptor signaling and alpha-toxin induced hemolysin was inhibited by selective blockers of P2X1 and P2X7 receptors [7]
Clostridium perfringens beta-toxin (CPB) is the cause of necrotic enteritis in animals including pigs, goats and sheep causing huge financial loses to agriculture industry
Summary
C. perfringens type C strain causes lethal infections such as necrotic enteritis and enterotoxaemia in small bowel of cattle, sheep, goats and humans. The amino acid residues involved in their interaction would be critical for CPB induced cytotoxicity and findings from this study may pave the way for designing and developing molecules to inhibit the interaction of CPB with the receptor and to control necrotic enteritis. Interactions energy of the generated CPB-P2X7 docked complex was assessed using PISA.
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