Computational Investigation of the Helicobacter pylori CagF Protein and Identification of Repurposable Drug Candidates through Protein–Protein Interaction Network Analysis

Abstract

CagF (Cag22) is an essential chaperone protein in Helicobacter pylori that plays a vital role in the stabilization and translocation of virulence factor CagA with the help of the type IV secretion system (T4SS). The protein contributes significantly to host-pathogen interactions. It is associated with the development of gastric diseases, along with gastric cancer. In this study, protein homology modeling, structure-based virtual screening of approved drugs, molecular docking and analysis of the CagF protein was performed. We employed a drug repurposing pipeline from which 10 compounds were shortlisted which helps to inhibit the CagA through CagF. Among the screened compounds, paliroden exhibited the most favourable predicted docking score (−9.3 kcal/mol) against the selected CagF binding pocket. The present study provides a computational pipeline for prioritizing candidate drug compounds for further investigation of CagF as a potential anti-virulence target.