Multiple amino acid substitutions in penicillin-binding protein-1A confer amoxicillin resistance in refractory Helicobacter pylori infection

J Microbiol Immunol Infect. 2023 Feb;56(1):40-47. doi: 10.1016/j.jmii.2022.07.006. Epub 2022 Aug 6.

Abstract

Background: Amoxicillin resistance in Helicobacter pylori is mainly associated with mutations in penicillin-binding protein-1A (PBP-1A). However, the specific amino acid substitutions in PBP-1A that confer amoxicillin resistance in H. pylori remain to be investigated.

Objective: This study aimed to investigate the molecular mechanism underlying amoxicillin resistance in patients with refractory H. pylori infection.

Methods: Esophagogastroduodenoscopy (EGD) was performed in patients with persistent H. pylori infection after at least two courses of H. pylori eradication therapy between January-2018 to March-2021. Refractory H. pylori was cultured from the gastric biopsy specimens. Antibiotic susceptibility testing was conducted to determine the minimum inhibitory concentrations (MICs). Sequence analysis of pbp-1A was performed for amoxicillin-resistant strains.

Results: Thirty-nine successfully cultured isolates were classified as refractory H. pylori isolates, and seventeen isolates were resistant to amoxicillin (MIC > 0.125 mg/L). Sequence analysis of resistant strains showed multiple mutations in the C-terminal region of PBP-1A that conferred amoxicillin resistance in H. pylori. However, the number of PBP-1A mutations did not correlate with the high MICs of amoxicillin-resistant isolates. Notably, some amino acid substitutions were identified in all Taiwanese isolates with history of eradication failure but not in published amoxicillin-susceptible strains, suggesting that the mutations may play a role in conferring antibiotic resistance to these strains.

Conclusions: Our results show that amoxicillin resistance in refractory H. pylori is highly correlated with numerous PBP-1A mutations that are strain specific. Continuous improvements in diagnostic tools, particularly molecular analysis approaches, can help to optimize current antimicrobial regimens.

Keywords: Amoxicillin; H. pylori; PBP-1A mutation; Refractory infection; Resistance.

MeSH terms

  • Amino Acid Substitution
  • Amoxicillin / pharmacology
  • Amoxicillin / therapeutic use
  • Anti-Bacterial Agents / pharmacology
  • Anti-Bacterial Agents / therapeutic use
  • Drug Resistance, Bacterial / genetics
  • Helicobacter Infections* / drug therapy
  • Helicobacter pylori* / genetics
  • Humans
  • Microbial Sensitivity Tests
  • Penicillin-Binding Proteins / genetics

Substances

  • Amoxicillin
  • Penicillin-Binding Proteins
  • Anti-Bacterial Agents