Multiple amino acid substitutions in penicillin-binding protein-1A confer amoxicillin resistance in refractory Helicobacter pylori infection
Copyright © 2022. Published by Elsevier B.V..
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.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2023 |
|---|---|
| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:56 |
|---|---|
| Enthalten in: |
Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi - 56(2023), 1 vom: 20. Feb., Seite 40-47 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Kuo, Chia-Jung [VerfasserIn] |
|---|
| Links: |
|---|
| Themen: |
804826J2HU |
|---|
| Anmerkungen: |
Date Completed 06.02.2023 Date Revised 06.02.2023 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1016/j.jmii.2022.07.006 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM345141784 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM345141784 | ||
| 003 | DE-627 | ||
| 005 | 20231226024407.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231226s2023 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.jmii.2022.07.006 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1150.xml |
| 035 | |a (DE-627)NLM345141784 | ||
| 035 | |a (NLM)35995672 | ||
| 035 | |a (PII)S1684-1182(22)00104-9 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Kuo, Chia-Jung |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Multiple amino acid substitutions in penicillin-binding protein-1A confer amoxicillin resistance in refractory Helicobacter pylori infection |
| 264 | 1 | |c 2023 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 06.02.2023 | ||
| 500 | |a Date Revised 06.02.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2022. Published by Elsevier B.V. | ||
| 520 | |a 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 | ||
| 520 | |a OBJECTIVE: This study aimed to investigate the molecular mechanism underlying amoxicillin resistance in patients with refractory H. pylori infection | ||
| 520 | |a 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 | ||
| 520 | |a 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 | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Amoxicillin | |
| 650 | 4 | |a H. pylori | |
| 650 | 4 | |a PBP-1A mutation | |
| 650 | 4 | |a Refractory infection | |
| 650 | 4 | |a Resistance | |
| 650 | 7 | |a Amoxicillin |2 NLM | |
| 650 | 7 | |a 804826J2HU |2 NLM | |
| 650 | 7 | |a Penicillin-Binding Proteins |2 NLM | |
| 650 | 7 | |a Anti-Bacterial Agents |2 NLM | |
| 700 | 1 | |a Ke, Jun-Nong |e verfasserin |4 aut | |
| 700 | 1 | |a Kuo, Tony |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Cheng-Yu |e verfasserin |4 aut | |
| 700 | 1 | |a Hsieh, Sen-Yung |e verfasserin |4 aut | |
| 700 | 1 | |a Chiu, Ya-Fang |e verfasserin |4 aut | |
| 700 | 1 | |a Wu, Hui-Yu |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Mei-Zi |e verfasserin |4 aut | |
| 700 | 1 | |a Bui, Ngoc-Niem |e verfasserin |4 aut | |
| 700 | 1 | |a Chiu, Cheng-Hsun |e verfasserin |4 aut | |
| 700 | 1 | |a Chiu, Cheng-Tang |e verfasserin |4 aut | |
| 700 | 1 | |a Lai, Chih-Ho |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi |d 1998 |g 56(2023), 1 vom: 20. Feb., Seite 40-47 |w (DE-627)NLM104271183 |x 1995-9133 |7 nnns |
| 773 | 1 | 8 | |g volume:56 |g year:2023 |g number:1 |g day:20 |g month:02 |g pages:40-47 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.jmii.2022.07.006 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 56 |j 2023 |e 1 |b 20 |c 02 |h 40-47 | ||