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Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus
BACKGROUND: Staphylococcus haemolyticus (S. haemolyticus) is the main etiological factor in skin and soft tissue infections (SSTI). S. haemolyticus infections are an important concern worldwide, especially with the associated biofilms and drug resistance. Herein, we investigated the inhibitory effec...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10540430/ https://www.ncbi.nlm.nih.gov/pubmed/37773054 http://dx.doi.org/10.1186/s12866-023-02997-5 |
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author | Liu, Jiaxin Liu, Ruijie Deng, Rongrong Zheng, Shiqian Shen, Zhibin |
author_facet | Liu, Jiaxin Liu, Ruijie Deng, Rongrong Zheng, Shiqian Shen, Zhibin |
author_sort | Liu, Jiaxin |
collection | PubMed |
description | BACKGROUND: Staphylococcus haemolyticus (S. haemolyticus) is the main etiological factor in skin and soft tissue infections (SSTI). S. haemolyticus infections are an important concern worldwide, especially with the associated biofilms and drug resistance. Herein, we investigated the inhibitory effect of Flavaspidic acid BB obtained from plant extractions on clinical S. haemolyticus strains and their biofilms. Moreover, we predicted its ability to bind to the protein-binding site by molecular simulation. Since the combination of Hsp70 and RNase P synthase after molecular simulation with flavaspidic acid BB is relatively stable, enzyme-linked immunosorbent assay (ELISA) was used to investigate Hsp70 and RNase P synthase to verify the potential antimicrobial targets of flavaspidic acid BB. RESULTS: The minimum inhibitory concentrations (MIC) of flavaspidic acid BB on 16 clinical strains of S. haemolyticus was 5 ~ 480 µg/mL, and BB had a slightly higher inhibitory effect on the biofilm than MUP. The inhibitory effect of flavaspidic acid BB on biofilm formation was better with an increase in the concentration of BB. Molecular simulation verified its ability to bind to the protein-binding site. The combination of ELISA kits showed that flavaspidic acid BB promoted the activity of Hsp70 and inhibited the activity of RNase P, revealing that flavaspidic acid BB could effectively inhibit the utilization and re-synthesis of protein and tRNA synthesis, thus inhibiting bacterial growth and biofilm formation to a certain extent. CONCLUSIONS: This study could potentially provide a new prospect for the development of flavaspidic acid BB as an antibacterial agent for resistant strains. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-023-02997-5. |
format | Online Article Text |
id | pubmed-10540430 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-105404302023-09-30 Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus Liu, Jiaxin Liu, Ruijie Deng, Rongrong Zheng, Shiqian Shen, Zhibin BMC Microbiol Research BACKGROUND: Staphylococcus haemolyticus (S. haemolyticus) is the main etiological factor in skin and soft tissue infections (SSTI). S. haemolyticus infections are an important concern worldwide, especially with the associated biofilms and drug resistance. Herein, we investigated the inhibitory effect of Flavaspidic acid BB obtained from plant extractions on clinical S. haemolyticus strains and their biofilms. Moreover, we predicted its ability to bind to the protein-binding site by molecular simulation. Since the combination of Hsp70 and RNase P synthase after molecular simulation with flavaspidic acid BB is relatively stable, enzyme-linked immunosorbent assay (ELISA) was used to investigate Hsp70 and RNase P synthase to verify the potential antimicrobial targets of flavaspidic acid BB. RESULTS: The minimum inhibitory concentrations (MIC) of flavaspidic acid BB on 16 clinical strains of S. haemolyticus was 5 ~ 480 µg/mL, and BB had a slightly higher inhibitory effect on the biofilm than MUP. The inhibitory effect of flavaspidic acid BB on biofilm formation was better with an increase in the concentration of BB. Molecular simulation verified its ability to bind to the protein-binding site. The combination of ELISA kits showed that flavaspidic acid BB promoted the activity of Hsp70 and inhibited the activity of RNase P, revealing that flavaspidic acid BB could effectively inhibit the utilization and re-synthesis of protein and tRNA synthesis, thus inhibiting bacterial growth and biofilm formation to a certain extent. CONCLUSIONS: This study could potentially provide a new prospect for the development of flavaspidic acid BB as an antibacterial agent for resistant strains. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-023-02997-5. BioMed Central 2023-09-29 /pmc/articles/PMC10540430/ /pubmed/37773054 http://dx.doi.org/10.1186/s12866-023-02997-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This 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/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Liu, Jiaxin Liu, Ruijie Deng, Rongrong Zheng, Shiqian Shen, Zhibin Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title | Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title_full | Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title_fullStr | Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title_full_unstemmed | Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title_short | Antibacterial activity and antibacterial mechanism of flavaspidic acid BB against Staphylococcus haemelyticus |
title_sort | antibacterial activity and antibacterial mechanism of flavaspidic acid bb against staphylococcus haemelyticus |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10540430/ https://www.ncbi.nlm.nih.gov/pubmed/37773054 http://dx.doi.org/10.1186/s12866-023-02997-5 |
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