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The rice foot rot disease caused by Dickeya oryzae is an important bacterial disease that could cause tremendous economic losses. The virulence factor modulating cluster (Vfm) quorum sensing (QS) system, a major virulence regulatory mechanism conserved in the Dickeya genus, controls the production of zeamines and various extracellular cell wall degradation enzymes in D. oryzae. In this study, we targeted the Vfm QS system of D. oryzae strain EC1 to screen for chemical compounds capable of attenuating its virulence. Using a high-throughput vfmE-lux reporter assay, we screened over 2000 compounds and identified a series of long aliphatic chain compounds - quaternary ammonium cationic surfactants (QACs) that substantially reduced the vfmE promoter activity. Further analysis revealed that QACs blocked strain EC1 response to Vfm signals. Quantitative PCR results showed that the transcriptional expression of the vfm gene cluster and its downstream virulence genes, including those encoding production of phytotoxin zeamines and CWDEs were significantly downregulated. Consistent with their role in blocking Vfm signaling, QACs markedly inhibited the production of virulence determinant zeamines and suppressed the secretion of cellulase and pectinase in strain EC1. Infection assays demonstrated that these compounds substantially reduced the virulence of D. oryzae EC1 toward rice seeds and alleviated the soft rot symptoms in potato tubers. This is the first report that QACs are potent inhibitors of the D. oryzae Vfm QS system, illustrating a promising QS-targeted approach for the control of bacterial rice foot rot disease.
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http://dx.doi.org/10.1016/j.pestbp.2025.106618 | DOI Listing |
Pestic Biochem Physiol
November 2025
State Key Laboratory of Green Pesticide, Integrative Microbiology Research Centre, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, College of Plant Protection, South China Agricultural University, Guangzhou 510642, China. Electronic address:
The rice foot rot disease caused by Dickeya oryzae is an important bacterial disease that could cause tremendous economic losses. The virulence factor modulating cluster (Vfm) quorum sensing (QS) system, a major virulence regulatory mechanism conserved in the Dickeya genus, controls the production of zeamines and various extracellular cell wall degradation enzymes in D. oryzae.
View Article and Find Full Text PDFSci Rep
August 2025
Porto Conte Ricerche S.R.L., Tramariglio, Alghero, Italy.
The ability of methicillin-resistant Staphylococcus aureus (MRSA) to adapt to environmental stressors is crucial for its survival and persistence. This study used shotgun proteomics to analyze the protein profiles of MRSA strains ST398 and JE2 under three experimental conditions: EC1 (control, 37 °C, pH 7), EC2 (35 °C, pH 6), and EC3 (35 °C, pH 6 with 5% NaCl). Proteins were extracted and digested with trypsin using filter-aided sample preparation (FASP), followed by LC-MS/MS analysis.
View Article and Find Full Text PDFNat Commun
July 2025
School of Basic Medical Sciences, Tsinghua University, Beijing, China.
PCDH10 is a newly identified general receptor for Western equine encephalitis virus (WEEV) members, a group of encephalitic alphaviruses that cause severe diseases in humans and equids. While WEEV typically binds PCDH10 as a receptor, nonpathogenic strains have evolved to lose mammalian PCDH10 binding, retaining only avian PCDH10 affinity. Virulent strains also engage VLDLR and ApoER2 as alternative receptors.
View Article and Find Full Text PDFJ Microbiol Biotechnol
June 2025
Zhejiang Province Key Laboratory of Plant Secondary Metabolism and Regulation, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, P.R. China.
Laccases (EC1.10.3.
View Article and Find Full Text PDFCell Rep
June 2025
National Laboratory of Biomacromolecules, Key Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences (CAS), Beijing 100101, P.R. China; University of Chinese Academy of Sciences, Beijing 100049, P.R. China. Electronic add
Western equine encephalitis virus (WEEV) enters cells via various receptors. Here, we report the cryoelectron microscopy (cryo-EM) structures of WEEV in complex with its receptors PCDH10 and very-low-density lipoprotein receptor (VLDLR). Structural analysis shows that PCDH10 binds in the cleft formed by adjacent E2-E1 heterodimers of WEEV through its EC1 ectodomain.
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