4.8 Article

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

Journal

NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-14685-3

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Funding

  1. National Institutes of Health, National Institute of Allergy and Infectious Diseases [AI137541, AI125429, AI126133, AI132996, R21 AI119368-01A1]
  2. Immunome
  3. Lankenau Institute for Medical Research
  4. National Institutes of Health, National Institute on Aging [5U01AG010483-20]

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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.

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