Diadenosine tetraphosphate modulated quorum sensing in bacteria treated with kanamycin.

Biofilm Diadenosine tetraphosphate Kanamycin Quorum sensing apaH

Journal

BMC microbiology
ISSN: 1471-2180
Titre abrégé: BMC Microbiol
Pays: England
ID NLM: 100966981

Informations de publication

Date de publication:
17 Nov 2023
Historique:
received: 14 09 2023
accepted: 06 11 2023
medline: 27 11 2023
pubmed: 18 11 2023
entrez: 18 11 2023
Statut: epublish

Résumé

The dinucleotide alarmone diadenosine tetraphosphate (Ap4A), which is found in cells, has been shown to affect the survival of bacteria under stress. Here, we labeled Ap4A with biotin and incubated the labeled Ap4A with the total proteins extracted from kanamycin-treated Escherichia coli to identify the Ap4A binding protein in bacteria treated with kanamycin. Liquid chromatography‒mass spectrometry (LCMS) and bioinformatics were used to identify novel proteins that Ap4A interacts with that are involved in biofilm formation, quorum sensing, and lipopolysaccharide biosynthesis pathways. Then, we used the apaH knockout strain of E. coli K12-MG1655, which had increased intracellular Ap4A, to demonstrate that Ap4A affected the expression of genes in these three pathways. We also found that the swarming motility of the apaH mutant strain was reduced compared with that of the wild-type strain, and under kanamycin treatment, the biofilm formation of the mutant strain decreased. These results showed that Ap4A can reduce the survival rate of bacteria treated with kanamycin by regulating quorum sensing (QS). These effects can expand the application of kanamycin combinations in the treatment of multidrug-resistant bacteria.

Sections du résumé

BACKGROUND BACKGROUND
The dinucleotide alarmone diadenosine tetraphosphate (Ap4A), which is found in cells, has been shown to affect the survival of bacteria under stress.
RESULTS RESULTS
Here, we labeled Ap4A with biotin and incubated the labeled Ap4A with the total proteins extracted from kanamycin-treated Escherichia coli to identify the Ap4A binding protein in bacteria treated with kanamycin. Liquid chromatography‒mass spectrometry (LCMS) and bioinformatics were used to identify novel proteins that Ap4A interacts with that are involved in biofilm formation, quorum sensing, and lipopolysaccharide biosynthesis pathways. Then, we used the apaH knockout strain of E. coli K12-MG1655, which had increased intracellular Ap4A, to demonstrate that Ap4A affected the expression of genes in these three pathways. We also found that the swarming motility of the apaH mutant strain was reduced compared with that of the wild-type strain, and under kanamycin treatment, the biofilm formation of the mutant strain decreased.
CONCLUSIONS CONCLUSIONS
These results showed that Ap4A can reduce the survival rate of bacteria treated with kanamycin by regulating quorum sensing (QS). These effects can expand the application of kanamycin combinations in the treatment of multidrug-resistant bacteria.

Identifiants

pubmed: 37978430
doi: 10.1186/s12866-023-03113-3
pii: 10.1186/s12866-023-03113-3
pmc: PMC10657157
doi:

Substances chimiques

Kanamycin 59-01-8
diadenosine tetraphosphate 5542-28-9
7-(N-(3-aminopropyl)amino)heptan-2-one 122269-09-4

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

353

Subventions

Organisme : Foundation of Guangdong Educational Committee for Youths
ID : 2019KQNCX150
Organisme : Applied Basic Research Programs of Science and Technology Commission Foundation of Guangdong Province
ID : 2022A1515012602
Organisme : Foundation of Guangdong Educational Committee for Characteristic Innovation
ID : 2023KTSCX146

Informations de copyright

© 2023. The Author(s).

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Auteurs

Xia Ji (X)

School of Life Science, Huizhou University, Huizhou, 516007, China. xiaji@hzu.edu.cn.

Ruojing Yu (R)

School of Life Science, Huizhou University, Huizhou, 516007, China.

Meilian Zhu (M)

School of Life Science, Huizhou University, Huizhou, 516007, China.

Cuilin Zhang (C)

School of Life Science, Huizhou University, Huizhou, 516007, China.

Libin Zhou (L)

School of Life Science, Huizhou University, Huizhou, 516007, China.

Tianshu Cai (T)

Huizhou Health Sciences Polytechnic, Huizhou, 516025, China.

Weiwei Li (W)

Huizhou Health Sciences Polytechnic, Huizhou, 516025, China.

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Classifications MeSH