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Updated: Aug 14, 2026

Quantitative Polymerase Chain Reaction (qPCR)-Based Rapid Diagnosis of Helicobacter pylori Infection and Antibiotic Resistance
Published on: July 28, 2023
Different penicillin-binding protein profiles in amoxicillin-resistant Helicobacter pylori
M P Dore1, D Y Graham, A R Sepulveda
1Department of Medicine and Pathology, VA Medical Center and Baylor College of Medicine, Houston, TX 77030, USA.
Background:
The beta-lactam group of antibiotics kills bacteria by inhibiting the terminal stages of peptidoglycan metabolism. We have recently identified amoxicillin-resistant Helicobacter pylori, none of which expressed beta-lactamase. Penicillin-binding proteins (PBPs) represent a group of target enzymes for the beta-lactam antibiotic family, and alterations in PBPs have been described in other penicillin-resistant bacteria. The amoxicillin-resistant phenotype characteristically was lost after freezing but could be restored by consecutive transfers into gradient plates.
Materials And Methods:
To determine whether amoxicillin resistance in H. pylori was related to alterations in any of the H. pylori PBPs, five H. pylori strains resistant to amoxicillin and three amoxicillin-sensitive strains were tested. PBPs were extracted from bacteria grown to logarithmic phase, labeled in vivo with 3H-benzylpenicillin, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography. Four main PBPs were separated from all amoxicillin-sensitive H. pylori strains.
Results:
Only three of the four main PBPs were found in the amoxicillin-resistant H. pylori strains. The differentially detectable PBP (PBP D) had an apparent molecular weight of 30 to 32 kD.
Conclusion:
These results suggest that PBP D might play a role in the amoxicillin-resistant phenotype of H. pylori strains lacking beta-lactamase activity.
Insights
Amoxicillin resistance in Helicobacter pylori may stem from alterations in penicillin-binding proteins (PBPs), specifically the absence of PBP D in resistant strains. This finding is crucial for understanding antibiotic resistance mechanisms.
Area of Science:
- Microbiology
- Antibiotic Resistance
- Bacterial Physiology
Background:
- Beta-lactam antibiotics inhibit bacterial peptidoglycan synthesis.
- Amoxicillin-resistant Helicobacter pylori strains lacking beta-lactamase were identified.
- Penicillin-binding proteins (PBPs) are targets for beta-lactams, and their alterations are linked to resistance.
Purpose of the Study:
- To investigate the potential role of altered penicillin-binding proteins (PBPs) in amoxicillin resistance in Helicobacter pylori.
- To compare PBPs between amoxicillin-sensitive and amoxicillin-resistant H. pylori strains.
Main Methods:
- Five amoxicillin-resistant and three sensitive H. pylori strains were analyzed.
- Penicillin-binding proteins (PBPs) were extracted and labeled in vivo with 3H-benzylpenicillin.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography were used to analyze PBPs.
Main Results:
- Four main PBPs were identified in amoxicillin-sensitive H. pylori strains.
- Amoxicillin-resistant strains exhibited only three of the four main PBPs.
- A specific PBP, designated PBP D (30-32 kD), was absent in resistant strains.
Conclusions:
- The absence or alteration of PBP D is implicated in the amoxicillin-resistant phenotype of beta-lactamase-negative H. pylori.
- PBP D is a potential key factor in amoxicillin resistance in H. pylori.
- Further research into PBP D function is warranted to understand amoxicillin resistance.
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