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Updated: Jan 18, 2026

In Vivo Imaging of Reactive Oxygen Species in a Murine Wound Model
Published on: November 17, 2018
Enterococcus faecalis redox metabolism activates the unfolded protein response to impair wound healing
Aaron Ming Zhi Tan1,2, Cenk Celik1, Stella Yue Ting Lee1
1School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Abstract:
Enterococcus faecalis is an opportunistic pathogen that thrives in biofilm-associated infections and delays wound healing, yet how it impairs host tissue responses is unclear. Here, we identified extracellular electron transport (EET) as a previously unrecognized source of reactive oxygen species (ROS) in E. faecalis and showed that this activity directly triggers the unfolded protein response (UPR) in epithelial cells and delays epithelial cell migration. ROS detoxification with catalase suppressed E. faecalis-induced UPR and rescued epithelial cell migration, while exogenous hydrogen peroxide was sufficient to restore UPR activation in EET-deficient strains. UPR disruption by pharmacological inhibition also impaired cell migration, highlighting a critical role for UPR homeostasis in wound repair. Our findings establish EET as a virulence mechanism that links bacterial redox metabolism to host cell stress and impaired repair, offering previously unidentified avenues for therapeutic intervention in chronic infections.
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