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


Amit Kumar Solanki#, Deepak Panwar#, Himani Kaushik & Lalit C. Garg*



National Institute of Immunology, New Delhi - 110067, India;



Dr. Lalit C. Garg - E-mail: lalit@nii.ac.in; lalitcgarg@gmail.com; Phone: +91
11 26703652; Fax: +91 11 26742125; ORCID ID: 0000 0001 6640 5383; *Corresponding author; #Equal contribution.


Article Type

Research Article



Received May 23, 2020; Revised June 23, 2020; Accepted June 23, 2020; Published August 31, 2020



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.



Clostridium perfringens, beta-toxin (CPB), molecular docking



Solanki et al. Bioinformation 16(8): 594-601 (2020)


Edited by

P Kangueane






Biomedical Informatics



This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.