Human listeriosis is caused by consuming foods contaminated with the bacterial pathogen , leading to the development of a severe and life-threatening foodborne illness. Detection of present in food and food processing environments is crucial for preventing infection. The peptidoglycan hydrolase IspC anchors non-covalently to the bacterial surface through its C-terminal cell wall-binding domain (CWBD), CWBD. This study explored the surface binding property of CWBD to design, construct, characterize, and assess an affinity molecular probe for detecting . CWBD recognized a cell wall ligand lipoteichoic acid that remains evenly displayed and mostly unoccupied on the bacterial surface for interaction with the exogenously added CWBD. CWBD, when fused to the enhanced green fluorescent protein reporter or covalently conjugated onto magnetic beads, exhibited the functionality as an antibody alternative for rapid detection and efficient separation of the pathogen.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10714868 | PMC |
http://dx.doi.org/10.1128/spectrum.05356-22 | DOI Listing |
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