Biology subjects

Konkel, M. E.

Publications and source records attributed to Konkel, M. E..

3 recordsLinked to original sources

bioRxiv2026

Artificial Intelligence of Things-Enhanced Automated Surveillance System for Global Antimicrobial Resistance in Food Supply Chain

Antimicrobial resistance (AMR) threatens food safety across the farm-to-fork continuum. Real-time surveillance is crucial to mitigate its global escalation, yet conventional antimicrobial susceptibility testing (AST) remains slow, labor-intensive, and impractical for large-scale monitoring. We developed an Artificial Intelligence of Things (AIoT)-integrated multiplex microfluidic platform enabling automated AMR surveillance of pathogens in food supply chain. Each node combines a single-board AIoT controller (Orange Pi 5B), portable incubator, colorimetric microfluidic chips, and environmental sensors, reducing costs by 98% compared with standard AST. A lightweight YOLOv5 model embedded in the controller achieved >99% accuracy in identifying bacterial growth and inhibition under antibiotic pressure, showing 96% and 95% agreement with standard results for Salmonella and Campylobacter, respectively. Data are synchronized to a cloud server for real-time aggregation and early resistance warning. This fully automated and low-cost system minimizes human error and workload, providing a scalable sample-to-answer solution for AMR surveillance in global agri-food system.

microbiology↗

bioRxiv2024

Metabolic conservation by protein quality control in Campylobacter jejuni underlies the antibiotic tolerance

Bacterial persistence enables survival during lethal antibiotic exposure and is implicated in recurrent infections, yet the physiology underlying bacterial persistence in many pathogens remains poorly defined. Here we show that exposure of Campylobacter jejuni to ampicillin or ciprofloxacin generates an antibiotic-persistent subpopulation. Rather than undergoing global metabolic shutdown, persister cells adopted a metabolically constrained state characterized by selective maintenance of oxidative phosphorylation and bioenergetic metabolism through coordinated proteostasis control. The ATP-dependent protease ClpP was essential for entry into this persistent state. Loss of ClpP disrupted proteostasis of the electron transport chain, specifically impaired bd-like terminal oxidase integrity, and reduced survival in vivo and in macrophages. These findings identify ClpP-dependent maintenance of redox and bioenergetic homeostasis as critical determinants of C. jejuni persistence and highlight metabolic remodeling as a defining feature of antibiotic tolerance. These insights may inform future therapeutic strategies aimed at disrupting persistence and improving antibiotic efficacy.

microbiology↗

bioRxiv2021

The Campylobacter jejuni CadF and FlpA fibronectin binding proteins facilitate signaling via host cell focal adhesions to inhibit cell motility and impede wound repair

Campylobacter jejuni is a major foodborne pathogen that exploits the focal adhesions of intestinal cells to promote invasion and cause severe gastritis. Focal adhesions are multiprotein complexes involved in bidirectional signaling between the actin cytoskeleton and the extracellular matrix. We investigated the dynamics of focal adhesion structure and function in C. jejuni infected cells using a comprehensive set of approaches, including confocal microscopy of live and fixed cells, immunoblots, and super-resolution iPALM. We found that C. jejuni infection of epithelial cells results in an increased focal adhesion size and altered topology. These changes resulted in a persistent modulatory effect on the host cell focal adhesion, as evidenced by an increase in cell adhesion strength, a decrease in individual cell motility, and a reduction of collective cell migration. We discovered that C. jejuni infection causes an increase in phosphorylation of paxillin and an alteration of paxillin turnover at the focal adhesion, which together represent a potential mechanistic basis for altered cell motility. Finally, we observed that infection of epithelial cells with the C. jejuni wild-type strain in the presence of protein synthesis inhibitor, a C. jejuni CadF and FlpA fibronectin-binding protein mutant, or a C. jejuni flagellar export mutant blunts paxillin phosphorylation and partially re-establishes individual host cell motility and collective cell migration. These findings provide a potential mechanism for the restricted intestinal repair observed in C. jejuni-infected animals and raise the possibility that bacteria targeting extracellular matrix components can alter cell behavior after binding and internalization by manipulating focal adhesions.

microbiology↗