FCCC LOGO Faculty Publications
Tursi SA , Puligedda RD , Szabo P , Nicastro LK , Miller AL , Qiu C , Gallucci S , Relkin NR , Buttaro BA , Dessain SK , Tukel C
Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli
Nat Commun. 2020 Feb 21;11(1) :1007
PMID: 32081907    PMCID: PMC7035420    URL: https://www.ncbi.nlm.nih.gov/pubmed/32081907
Back to previous list
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.
2041-1723 Tursi, Sarah A Puligedda, Rama Devudu Szabo, Paul Nicastro, Lauren K Miller, Amanda L Qiu, Connie ORCID: http://orcid.org/0000-0002-1623-9871 Gallucci, Stefania Relkin, Norman R Buttaro, Bettina A Dessain, Scott K Tukel, Cagla ORCID: http://orcid.org/0000-0001-7073-0226 Journal Article England Nat Commun. 2020 Feb 21;11(1):1007. doi: 10.1038/s41467-020-14685-3.