<p><i>Helicobacter pylori</i> (<i>H. pylori</i>) is a short, helical-shaped gram-negative bacterium found mostly in the stomach’s pyloric region, and is associated with gastrointestinal disorders like gastritis, peptic ulcers and gastric cancer. Protein–protein interactions between <i>H. pylori</i> and human are crucial molecular events during infection, where proteins from the pathogen interact with host proteins to facilitate disease. Thus, identifying host–pathogen protein–protein interactions (HP-PPIs) can decipher the underlying mechanism of disease which is vital for discovering new drug targets to combat <i>H. pylori</i> infection. In this quest, we utilized experimentally reported intra-species PPI data and used advanced computational methods to map host–pathogen PPIs between <i>H. pylori</i> and a human host. The core network consists of 449 interactions involving 176 human and 78 <i>H. pylori</i> proteins. Analysis of the network reveals 12 key functional modules associated with the HP-PPIs. Further analysis finds 8 hub proteins that likely play crucial roles in the pathogenesis of <i>H. pylori.</i> Functional analysis revealed that <i>H. pylori</i> proteins are involved in ATP-dependent activity, binding activity and transporter activity. Whereas the human proteins are involved in apoptosis, toll like receptor signalling and inflammation. Pathway analysis demonstrated that the <i>H. pylori</i> proteins are involved in ATP synthesis and glycolysis. Thus, the results of functional and pathway analysis confirm that the reported proteins are critical to the host–pathogen interface. Overall, this study provides the core HP-PPI network between <i>H. Pylori</i> and human, and reports eight proteins that are vital for the infection process. Thus, this work provides new insights into the mechanism of host–pathogen interaction that would guide the experimentalists for further exploration of the underlying mechanism of <i>H. pylori</i> infection.</p>

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Network analysis of protein–protein interactions between human and Helicobacter pylori reveals key proteins involved in the host–pathogen interface

  • Monika Tiwari,
  • Anup Som

摘要

Helicobacter pylori (H. pylori) is a short, helical-shaped gram-negative bacterium found mostly in the stomach’s pyloric region, and is associated with gastrointestinal disorders like gastritis, peptic ulcers and gastric cancer. Protein–protein interactions between H. pylori and human are crucial molecular events during infection, where proteins from the pathogen interact with host proteins to facilitate disease. Thus, identifying host–pathogen protein–protein interactions (HP-PPIs) can decipher the underlying mechanism of disease which is vital for discovering new drug targets to combat H. pylori infection. In this quest, we utilized experimentally reported intra-species PPI data and used advanced computational methods to map host–pathogen PPIs between H. pylori and a human host. The core network consists of 449 interactions involving 176 human and 78 H. pylori proteins. Analysis of the network reveals 12 key functional modules associated with the HP-PPIs. Further analysis finds 8 hub proteins that likely play crucial roles in the pathogenesis of H. pylori. Functional analysis revealed that H. pylori proteins are involved in ATP-dependent activity, binding activity and transporter activity. Whereas the human proteins are involved in apoptosis, toll like receptor signalling and inflammation. Pathway analysis demonstrated that the H. pylori proteins are involved in ATP synthesis and glycolysis. Thus, the results of functional and pathway analysis confirm that the reported proteins are critical to the host–pathogen interface. Overall, this study provides the core HP-PPI network between H. Pylori and human, and reports eight proteins that are vital for the infection process. Thus, this work provides new insights into the mechanism of host–pathogen interaction that would guide the experimentalists for further exploration of the underlying mechanism of H. pylori infection.