Helicobacter pylori (Hp) is associated in human gastric diseases. It touches more than 50% of the world's population. Clinically, amoxicillin is one of the antibiotics used to treat the pathogenic agent. It inhibits bacterial wall synthesis, by blocking the transpeptidase domain of penicillin binding protein 1A (PBP1A). Mutations in this domain are responsible for antimicrobial resistance (AMR). The transglycosylase domain is necessary to activate the transpeptidase. But its part in the resistance remains little documented. The objective of this study was to analyze the protein sequence of this domain in samples of Malian patients. Therefore, the PCR product was sequenced from five Hp positive samples. After alignment with the Helicobacter pylori 26695 sequence (reference), several amino acid substitutions were identified: T30N / F67S / I79V / I101V / F125L / I148L for sample 1 (PBP1A-ML1); G44S / I101V / F125L for PBP1A-ML2 and PBP1A-ML5 and A36V / F125L / I148L for PBP1A-ML3 and PBP1A-ML4. The last two groups of mutations were also observed in Hp PBP1A from other continents. Their existence shows the distribution of two or more Hp strains in Mali and worldwide. Although their direct implications for AMR have not been demonstrated, but their presence is supposed to modify the affinity of amoxicillin for its target. Considering the importance of transglycosylase in the activation of the transpeptidase domain, substitutions would allow Hp to adapt to a change in its environment. Additional research is needed to identify the role of observed substitutions.
| Published in | American Journal of Biomedical and Life Sciences (Volume 10, Issue 6) |
| DOI | 10.11648/j.ajbls.20221006.11 |
| Page(s) | 155-161 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2022. Published by Science Publishing Group |
Helicobacter pylori, Amoxicillin, PBP1A, Transglycosylase Domain, Diversity, Mali
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APA Style
David Guindo, Alpha Seydou Yaro, Astan Traore, Yaya Bouare, Bernard Sodio. (2022). Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and Helicobacter pylori. American Journal of Biomedical and Life Sciences, 10(6), 155-161. https://doi.org/10.11648/j.ajbls.20221006.11
ACS Style
David Guindo; Alpha Seydou Yaro; Astan Traore; Yaya Bouare; Bernard Sodio. Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and Helicobacter pylori. Am. J. Biomed. Life Sci. 2022, 10(6), 155-161. doi: 10.11648/j.ajbls.20221006.11
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Download@article{10.11648/j.ajbls.20221006.11,
author = {David Guindo and Alpha Seydou Yaro and Astan Traore and Yaya Bouare and Bernard Sodio},
title = {Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and Helicobacter pylori},
journal = {American Journal of Biomedical and Life Sciences},
volume = {10},
number = {6},
pages = {155-161},
doi = {10.11648/j.ajbls.20221006.11},
url = {https://doi.org/10.11648/j.ajbls.20221006.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbls.20221006.11},
abstract = {Helicobacter pylori (Hp) is associated in human gastric diseases. It touches more than 50% of the world's population. Clinically, amoxicillin is one of the antibiotics used to treat the pathogenic agent. It inhibits bacterial wall synthesis, by blocking the transpeptidase domain of penicillin binding protein 1A (PBP1A). Mutations in this domain are responsible for antimicrobial resistance (AMR). The transglycosylase domain is necessary to activate the transpeptidase. But its part in the resistance remains little documented. The objective of this study was to analyze the protein sequence of this domain in samples of Malian patients. Therefore, the PCR product was sequenced from five Hp positive samples. After alignment with the Helicobacter pylori 26695 sequence (reference), several amino acid substitutions were identified: T30N / F67S / I79V / I101V / F125L / I148L for sample 1 (PBP1A-ML1); G44S / I101V / F125L for PBP1A-ML2 and PBP1A-ML5 and A36V / F125L / I148L for PBP1A-ML3 and PBP1A-ML4. The last two groups of mutations were also observed in Hp PBP1A from other continents. Their existence shows the distribution of two or more Hp strains in Mali and worldwide. Although their direct implications for AMR have not been demonstrated, but their presence is supposed to modify the affinity of amoxicillin for its target. Considering the importance of transglycosylase in the activation of the transpeptidase domain, substitutions would allow Hp to adapt to a change in its environment. Additional research is needed to identify the role of observed substitutions.},
year = {2022}
}
TY - JOUR T1 - Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and Helicobacter pylori AU - David Guindo AU - Alpha Seydou Yaro AU - Astan Traore AU - Yaya Bouare AU - Bernard Sodio Y1 - 2022/11/04 PY - 2022 N1 - https://doi.org/10.11648/j.ajbls.20221006.11 DO - 10.11648/j.ajbls.20221006.11 T2 - American Journal of Biomedical and Life Sciences JF - American Journal of Biomedical and Life Sciences JO - American Journal of Biomedical and Life Sciences SP - 155 EP - 161 PB - Science Publishing Group SN - 2330-880X UR - https://doi.org/10.11648/j.ajbls.20221006.11 AB - Helicobacter pylori (Hp) is associated in human gastric diseases. It touches more than 50% of the world's population. Clinically, amoxicillin is one of the antibiotics used to treat the pathogenic agent. It inhibits bacterial wall synthesis, by blocking the transpeptidase domain of penicillin binding protein 1A (PBP1A). Mutations in this domain are responsible for antimicrobial resistance (AMR). The transglycosylase domain is necessary to activate the transpeptidase. But its part in the resistance remains little documented. The objective of this study was to analyze the protein sequence of this domain in samples of Malian patients. Therefore, the PCR product was sequenced from five Hp positive samples. After alignment with the Helicobacter pylori 26695 sequence (reference), several amino acid substitutions were identified: T30N / F67S / I79V / I101V / F125L / I148L for sample 1 (PBP1A-ML1); G44S / I101V / F125L for PBP1A-ML2 and PBP1A-ML5 and A36V / F125L / I148L for PBP1A-ML3 and PBP1A-ML4. The last two groups of mutations were also observed in Hp PBP1A from other continents. Their existence shows the distribution of two or more Hp strains in Mali and worldwide. Although their direct implications for AMR have not been demonstrated, but their presence is supposed to modify the affinity of amoxicillin for its target. Considering the importance of transglycosylase in the activation of the transpeptidase domain, substitutions would allow Hp to adapt to a change in its environment. Additional research is needed to identify the role of observed substitutions. VL - 10 IS - 6 ER -
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