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Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants
Mycoplasma pneumoniae is one of the leading causes of community-acquired pneumonia in children and adolescents. Because of the wide application of macrolides in clinical treatment, macrolide-resistant M. pneumoniae strains have become increasingly common worldwide. However, the molecular mechanisms...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7881084/ https://www.ncbi.nlm.nih.gov/pubmed/33580372 http://dx.doi.org/10.1186/s13568-021-01187-8 |
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author | Li, Shaoli Xue, Guanhua Zhao, Hanqing Feng, Yanling Yan, Chao Cui, Jinghua Xie, Xianghui Yuan, Jing |
author_facet | Li, Shaoli Xue, Guanhua Zhao, Hanqing Feng, Yanling Yan, Chao Cui, Jinghua Xie, Xianghui Yuan, Jing |
author_sort | Li, Shaoli |
collection | PubMed |
description | Mycoplasma pneumoniae is one of the leading causes of community-acquired pneumonia in children and adolescents. Because of the wide application of macrolides in clinical treatment, macrolide-resistant M. pneumoniae strains have become increasingly common worldwide. However, the molecular mechanisms underlying drug resistance in M. pneumoniae are poorly understood. In the present work, we analyzed the whole proteomes of macrolide-sensitive and macrolide-resistant strains of M. pneumoniae using a tandem mass tag-labeling quantitative proteomic technique, Data are available via ProteomeXchange with identifier PXD022220. In total, 165 differentially expressed proteins were identified, of which 80 were upregulated and 85 were downregulated in the drug-resistant strain compared with the sensitive strain. Functional analysis revealed that these proteins were predominantly involved in protein and peptide biosynthesis processes, the ribosome, and transmembrane transporter activity, which implicates them in the mechanism(s) of resistance of M. pneumoniae to macrolides. Our results provide new insights into drug resistance in M. pneumoniae and identify potential targets for further studies on resistance mechanisms in this bacterium. |
format | Online Article Text |
id | pubmed-7881084 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-78810842021-02-25 Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants Li, Shaoli Xue, Guanhua Zhao, Hanqing Feng, Yanling Yan, Chao Cui, Jinghua Xie, Xianghui Yuan, Jing AMB Express Original Article Mycoplasma pneumoniae is one of the leading causes of community-acquired pneumonia in children and adolescents. Because of the wide application of macrolides in clinical treatment, macrolide-resistant M. pneumoniae strains have become increasingly common worldwide. However, the molecular mechanisms underlying drug resistance in M. pneumoniae are poorly understood. In the present work, we analyzed the whole proteomes of macrolide-sensitive and macrolide-resistant strains of M. pneumoniae using a tandem mass tag-labeling quantitative proteomic technique, Data are available via ProteomeXchange with identifier PXD022220. In total, 165 differentially expressed proteins were identified, of which 80 were upregulated and 85 were downregulated in the drug-resistant strain compared with the sensitive strain. Functional analysis revealed that these proteins were predominantly involved in protein and peptide biosynthesis processes, the ribosome, and transmembrane transporter activity, which implicates them in the mechanism(s) of resistance of M. pneumoniae to macrolides. Our results provide new insights into drug resistance in M. pneumoniae and identify potential targets for further studies on resistance mechanisms in this bacterium. Springer Berlin Heidelberg 2021-02-12 /pmc/articles/PMC7881084/ /pubmed/33580372 http://dx.doi.org/10.1186/s13568-021-01187-8 Text en © The Author(s) 2021 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Original Article Li, Shaoli Xue, Guanhua Zhao, Hanqing Feng, Yanling Yan, Chao Cui, Jinghua Xie, Xianghui Yuan, Jing Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title | Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title_full | Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title_fullStr | Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title_full_unstemmed | Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title_short | Quantitative proteomics analysis of Mycoplasma pneumoniae identifies potential macrolide resistance determinants |
title_sort | quantitative proteomics analysis of mycoplasma pneumoniae identifies potential macrolide resistance determinants |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7881084/ https://www.ncbi.nlm.nih.gov/pubmed/33580372 http://dx.doi.org/10.1186/s13568-021-01187-8 |
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