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DC Field | Value | Language |
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dc.contributor.author | Kuo, Chia-Jung | - |
dc.contributor.author | Ke, Jun-Nong | - |
dc.contributor.author | Kuo, Tony | - |
dc.contributor.author | Lin, Cheng-Yu | - |
dc.contributor.author | Hsieh, Sen-Yung | - |
dc.contributor.author | Chiu, Ya-Fang | - |
dc.date.accessioned | 2024-12-16T03:45:59Z | - |
dc.date.available | 2024-12-16T03:45:59Z | - |
dc.date.issued | 2023-02 | - |
dc.identifier.citation | Original Article | en_US |
dc.identifier.uri | http://localhost:8080/xmlui/handle/123456789/9106 | - |
dc.description.abstract | 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. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Journal of Microbiology, Immunology and Infection | en_US |
dc.subject | Refractory infection | en_US |
dc.subject | H. pylori | en_US |
dc.subject | Amoxicillin | en_US |
dc.title | Multiple amino acid substitutions in penicillin-binding protein-1A confer amoxicillin resistance in refractory Helicobacter pylori infection | en_US |
dc.type | Article | en_US |
Appears in Collections: | VOL 56 NO 1 2023 |
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