Multiple Helicobacter pylori and bacterial proteins

Multiple Helicobacter pylori and bacterial proteins refers to the diverse set of molecular targets within the Helicobacter pylori bacterium and associated microflora that are addressed during antimicrobial therapy. Helicobacter pylori is a Gram-negative, spiral-shaped bacterium that colonizes the human stomach, where it is a primary cause of chronic gastritis, peptic ulcers, and gastric adenocarcinoma (Polk & Peek, 2010, Nature Reviews Cancer). Essential targets within this group include the enzyme urease, which allows the bacterium to survive the acidic gastric environment by producing ammonia, and various proteins involved in cell wall synthesis (penicillin-binding proteins) and protein translation (ribosomal subunits) (Mobley et al., 1995, Microbiological Reviews). Clinical management typically employs triple or quadruple therapy, combining antibiotics like amoxicillin, clarithromycin, and metronidazole with proton pump inhibitors to inhibit these bacterial proteins and eradicate the infection (Malfertheiner et al., 2023, The Lancet). The use of multiple targets is a strategic necessity to combat the high rate of antibiotic resistance observed in H. pylori strains globally (Megraud et al., 2021, Gut).

Other names

H. pylori proteinsHelicobacter pylori proteomeBacterial targets in H. pylori infectionUrease and other H. pylori proteins

The mechanism of action involves the simultaneous inhibition of various essential bacterial processes, including cell wall synthesis (via penicillin-binding proteins), protein synthesis (via the 50S and 30S ribosomal subunits), and DNA integrity (via nitroreductase-mediated activation of prodrugs), as well as the neutralization of survival enzymes like urease (Malfertheiner et al., 2023, The Lancet; Megraud et al., 2021, Gut).