Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli

Sarah A. Tursi, Rama Devudu Puligedda, Paul Szabo, Lauren K. Nicastro, Amanda L. Miller, Connie Qiu, Stefania Gallucci, Norman R. Relkin, Bettina A. Buttaro, Scott K. Dessain () and Çagla Tükel ()
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Sarah A. Tursi: Temple University
Rama Devudu Puligedda: Lankenau Institute for Medical Research
Paul Szabo: Weill Cornell Medical Feil Family Brain & Mind Research Institute
Lauren K. Nicastro: Temple University
Amanda L. Miller: Temple University
Connie Qiu: Temple University
Stefania Gallucci: Temple University
Norman R. Relkin: Weill Cornell Medical Feil Family Brain & Mind Research Institute
Bettina A. Buttaro: Temple University
Scott K. Dessain: Lankenau Institute for Medical Research
Çagla Tükel: Temple University

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract Bacterial biofilms, especially those associated with implanted medical devices, are difficult to eradicate. Curli amyloid fibers are important components of the biofilms formed by the Enterobacteriaceae family. Here, we show that a human monoclonal antibody with pan-amyloid-binding activity (mAb 3H3) can disrupt biofilms formed by Salmonella enterica serovar Typhimurium in vitro and in vivo. The antibody disrupts the biofilm structure, enhancing biofilm eradication by antibiotics and immune cells. In mice, 3H3 injections allow antibiotic-mediated clearance of catheter-associated S. Typhimurium biofilms. Thus, monoclonal antibodies that bind a pan-amyloid epitope have potential to prevent or eradicate bacterial biofilms.

Date: 2020
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DOI: 10.1038/s41467-020-14685-3

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