Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and <i>Helicobacter pylori</i>

David Guindo; Alpha Seydou Yaro; Astan Traore; Yaya Bouare; Bernard Sodio

doi:doi:10.11648/j.ajbls.20221006.11

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Mutation in Transglycosylase Domain of Penicillin Binding Protein 1A (PBP1A) and Helicobacter pylori

David Guindo, Alpha Seydou Yaro, Astan Traore, Yaya Bouare, Bernard Sodio

Published in American Journal of Biomedical and Life Sciences (Volume 10, Issue 6)

Received: 10 October 2022 Accepted: 27 October 2022 Published: 4 November 2022

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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.

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), 2024. Published by Science Publishing Group

Keywords

Helicobacter pylori, Amoxicillin, PBP1A, Transglycosylase Domain, Diversity, Mali

References

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[9]	Attaran B, Salehi N, Ghadiri B, Esmaeili M, Kalateh S, Tashakoripour M, et al. The penicillin binding protein 1a of Helicobacter pylori, its amoxicillin binding site and access routes. Gut Pathog. Dec 2021; 13 (1): 43.
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[14]	Tran TT, Nguyen AT, Quach DT, Pham DTH, Cao NM, Nguyen UTH, et al. Emergence of amoxicillin resistance and identification of novel mutations of the pbp1a gene in Helicobacter pylori in vietnam. BMC Microbiol. 2022; 22 (1): 41.
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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

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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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AMA 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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@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}
}

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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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Author Information

David Guindo

Applied Microbiology Laboratory, University of Sciences, Techniques and Technologies of Bamako, Bamako, Mali
Alpha Seydou Yaro

Department of Biology, Faculty of Sciences and Techniques, University of Sciences, Techniques and Technologies of Bamako, Bamako, Mali
Astan Traore

Department of Biology, Faculty of Sciences and Techniques, University of Sciences, Techniques and Technologies of Bamako, Bamako, Mali
Yaya Bouare

Department of Biology, Faculty of Sciences and Techniques, University of Sciences, Techniques and Technologies of Bamako, Bamako, Mali
Bernard Sodio

Department of Biology, Faculty of Sciences and Techniques, University of Sciences, Techniques and Technologies of Bamako, Bamako, 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

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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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AMA 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

Copy | 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}
}

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