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


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.

SUBMITTER: Tursi SA 

PROVIDER: S-EPMC7035420 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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

Tursi Sarah A SA   Puligedda Rama Devudu RD   Szabo Paul P   Nicastro Lauren K LK   Miller Amanda L AL   Qiu Connie C   Gallucci Stefania S   Relkin Norman R NR   Buttaro Bettina A BA   Dessain Scott K SK   Tükel Çagla Ç  

Nature communications 20200221 1


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 cell  ...[more]

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