| Sign up

PDF (12.8 MB)

Cite

Collect

Submit Manuscript

Show Outline

Figures (11)

Fig. 1

Fig. 2

Fig. 3

Fig. 4

Fig. 5

Fig. 6

Fig. 7

Fig. 8

Fig. 9

Tables (2)

Table 1

Table 2

Article | Open Access

Sesamol: a novel quorum sensing inhibitor and colistin accelerator against Pseudomonas aeruginosa

Pengcheng Ji^¹, Kunyuan Yin^¹, Yue Jiang, Yulu Sun, Wenqi Luo, Jinwei Zhou()

School of Food and Biological Engineering, Xuzhou University of Technology, Xuzhou 221018, China

¹ These authors contributed equally to this work.

Peer review under responsibility of Beijing Academy of Food Sciences.

Show Author Information

Highlights

• Sesamol reduced virulence factors production and enhance the susceptibility of biofilm cells to colistin.

• Sesamol down-regulated the expressions of genes involved in QS, virulence, and oxidative stress.

• Sesamol intensified oxidative stress and enhanced the permeability of membrane.

• Sesamol treatment resulted in the disorder of amino acid metabolism and energy metabolism.

• Sesamol has the potential to function as a potent anti-virulence agent to defend against spoilage P. aeruginosa.

Graphical Abstract

View original image Download original image

Abstract

We assessed the quorum sensing (QS) inhibitory impact of sesamol against the foodborne bacterium Pseudomonas aeruginosa. At concentrations ranging from 50 to 200 μg/mL, sesamol significantly inhibited the production of virulence factors such as protease, elastase, pyocyanin, rhamnolipid, and chemotaxis, and improved the susceptibility of bacterial and biofilm cells to colistin. Integrated transcriptomics, metabolomics, and docking analyses indicated that exposure to sesamol destroyed the QS system and down-regulated the expressions of genes encoding virulence and antioxidant enzymes. The down-regulation of genes encoding antioxidant enzymes intensified oxidative stress, as demonstrated by the enhancement of reactive oxygen species and H₂O₂. The enhanced oxidative stress changed the components of the cell membrane, improved its permeability, and ultimately enhanced the susceptibility of bacterial and biofilm cells to colistin. Moreover, exposure to sesamol also led to the disorder of amino acid metabolism and energy metabolism, eventually attenuating the pathogenicity of P. aeruginosa. These findings indicated that sesamol can function as a potent anti-virulence agent to defend against food spoilage caused by P. aeruginosa.

Keywords

Sesamol Pseudomonas aeruginosaQuorum sensing Virulence Biofilm

Electronic Supplementary Material

Download File(s)

fshw-14-3-9250075_ESM.docx (32.4 KB)

References

[1]

C.B. Penha, E. Bonin, A.F. da Silva, et al., Photodynamic inactivation of foodborne and food spoilage bacteria by curcumin, LWT-Food Sci. Technol. 76 (2017) 198-202. https://doi.org/10.1016/j.lwt.2016.07.037.

Gene category	Name	log₂ FC	Gene description
Phenazine biosynthesis
PA1899	phzA2	−2.99	Phenazine biosynthesis
PA1900	phzB2	−2.45	Phenazine biosynthesis
PA1901	phzC2	−2.35	Phenazine biosynthesis
PA1902	phzD2	−1.13	Phenazine biosynthesis
PA4213	phzD1	−1.13	Phenazine biosynthesis
PA4214	phzE1	−1.07	Phenazine biosynthesis
PA1903	phzE2	−1.07	Phenazine biosynthesis
PA1905	phzG2	−2.97	Phenazine biosynthesis
QS
PA3477	rhlR	−1.70	Transcriptional regulator RhlR
Virulence factors
PA3479	rhlA	−2.08	Rhamnosyltransferase subunit A
PA3478	rhlB	−1.90	Rhamnosyltransferase subunit B
PA1871	lasA	−2.07	Protease LasA
PA3724	lasB	−2.00	Elastase LasB
PA2570	lecA	−2.95	PA-I galactophilic lectin
PA3361	lecB	−1.96	Fucose-binding lectin PA-IIL
PA3350	PA3350	−1.58	Flagellar basal body P-ring biosynthesis protein FlgA
PA1100	fliE	−1.91	Flagellar hook-basal body complex protein FliE
PA1101	fliF	−1.37	Flagellar MS-ring protein
PA1452	flhA	−2.10	Flagellar biosynthesis protein FlhA
Biofilm formation
PA2231	pslA	−1.16	Biofilm formation protein PslA
Cationic antimicrobial peptide resistance
PA1249	aprA	−1.20	Alkaline metalloproteinase
Oxidative stress
PA2826	PA2826	−2.76	Glutathione peroxidase
PA4613	katB	−3.75	Catalase
TCA cycle
PA2250	lpdV	1.02	Dihydrolipoyl dehydrogenase
PA1580	gltA	1.55	Citrate synthase
PA2623	icd	1.17	Isocitrate dehydrogenase
PA2624	idh	2.14	Isocitrate dehydrogenase
PA1583	sdhA	1.09	Succinate dehydrogenase flavoprotein subunit
PA1584	sdhB	1.11	Succinate dehydrogenase iron-sulfur subunit
PA1589	sucD	1.27	Succinyl-CoA ligase subunit α
PA1588	sucC	1.39	Succinyl-CoA ligase subunit β
Bacterial secretion system
PA1512	hcpA	−3.82	Secreted protein Hcp
PA5267	hcpB	−3.54	Secreted protein Hcp
PA1666	PA1666	−2.51	Hypothetical protein

No.	Compound	Assignments	Chemical shift^a (10^-6)	FC^b	P^c
Note: ^a Multiplicity: (s) singlet, (d) doublet, (t) triplet, (q) quartets, (m) multiplets; ^b color-coded according to the log₂ FC: red and blue represent the increased and decreased metabolites, respectively, in Ses-treated group; ^c P values were calculated based on a parametric Student t-test or a nonparametric Mann-Whitney test and were corrected by the Benjamini-Hochberg (BH) methods; values with asterisk symbols denoted extent of significance: P < 0.05, P < 0.01, and **P < 0.001.
1	2-Hydroxyvalerate	CH₃	1.27 (d)	−0.27	***
2	Isoleucine	δ-CH₃, γ-CH₃, α-CH	0.94 (t), 1.01 (d), 3.67 (d)	−0.86	***
3	Leucine	δ-CH₃, γ-CH₃, α-CH	0.96 (t), 0.97 (d), 3.72 (d)	−0.21	***
4	Valine	γ-CH₃, γ-CH₃, α-CH	0.99 (d), 1.05 (d), 3.59 (d)	−0.17	**
5	Lactate	CH₃	1.33 (d)	0.20	*
6	Putrescine	NH₂	1.70 (m)	−0.08
7	Acetate	CH₃	1.92 (s)	0.75	**
8	Methionine	2-CH₃, 4-CH₂, 3-CH₂	2.14 (m), 2.65 (t)	−0.02
9	4-Aminobutyrate	β-CH₂, α-CH₂, γ-CH₂	1.91 (m), 2.30 (t), 3.01 (t)	0.31	**
10	Glutamate	β-CH₂, γ-CH₂, α-CH	2.06 (m), 2.35 (dt), 3.76 (m)	−0.12	*
11	Succinate	CH₂	2.41 (s)	0.47	*
12	Ethanolamine	CH₂	3.13 (t), 3.81 (t)	0.02
13	Choline	CH₃	3.21 (s)	−0.11	*
14	Carnitine	CH₃	3.19 (s)	−0.26	**
15	Betaine	CH₂	3.23 (s)	−0.26	*
16	Homoserine	CH	3.84 (t)	0.18	**
17	Uracil	CH	5.81 (d), 7.54 (d)	0.23	**
18	UDP-glucose	CH	5.97 (d)	0.17	*
19	AMP	2-CH	6.15 (s)	0.10
20	Fumarate	CH	6.52 (s)	0.95	**
21	Tyrosine	2-CH, 6-CH	6.91 (d)	−0.30	**
22	Phenylalanine	ph-H	7.30-7.46 (m)	0.11