Helicobacter pylori iron acquisition and iron-binding proteins

Helicobacter pylori iron acquisition and iron-binding proteins are essential for the survival, colonization, and virulence of the bacterium in the human gastric mucosa. Since iron is a vital cofactor for metabolic processes but is sequestered by host proteins, H. pylori utilizes a complex network of TonB-dependent transporters such as FrpB and FecA, the ferrous iron transporter FeoB, and heme-scavenging systems to meet its requirements (PubMed: 11133958, 10913087). Once inside the cell, iron is stored in proteins like the ferritin-like protein (Pfr) and neutrophil-activating protein (NapA), which also protect the bacterium from oxidative damage (PubMed: 8655507, 10490020). These systems are tightly regulated by the Ferric Uptake Regulator (Fur) to prevent toxicity and maintain homeostasis. Because these pathways are distinct from human iron metabolism and are crucial for infection, they represent attractive targets for novel antimicrobial agents. Bismuth-based drugs and iron mimetics like gallium have been shown to disrupt these iron acquisition mechanisms, effectively inducing bacterial iron starvation and death (PubMed: 10572111, 30254114).

Other names

Helicobacter pylori iron uptake systemH. pylori iron metabolism proteinsH. pylori iron homeostasis machinery

Inhibition of iron acquisition through competitive binding, disruption of iron transport mechanisms, or interference with iron-dependent regulatory proteins to induce bacterial iron starvation or toxicity.