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

Author

Listed:
  • 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)

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.

Suggested Citation

  • 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 & Çagla Tükel, 2020. "Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14685-3
    DOI: 10.1038/s41467-020-14685-3
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