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Molecular docking analysis of P2X7 receptor with the beta toxin from Clostridium perfringens.

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.

SUBMITTER: Solanki AK

PROVIDER: S-EPMC7649019 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Molecular docking analysis of P2X7 receptor with the beta toxin from Clostridium perfringens.

Solanki Amit Kumar AK Panwar Deepak D Kaushik Himani H Garg Lalit C LC

Bioinformation 20200831 8

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 ...[more]

PMID: 33214747

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