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Bacterial DNABII family proteins, primarily comprising Integration Host Factor (IHF) and Histone-like protein (HU), are highly conserved nucleoid-associated proteins essential for bacterial physiology (Goodman et al., 2011, PubMed). Intracellularly, they facilitate DNA bending and compaction, playing vital roles in replication, recombination, and gene regulation. Extracellularly, these proteins serve as critical structural linchpins within the biofilm matrix by binding and stabilizing the junctions of extracellular DNA (eDNA) scaffolds (Novotny et al., 2013, PubMed). Therapeutic strategies targeting DNABII proteins, such as the monoclonal antibody TRL1068, aim to disrupt this structural integrity, causing the biofilm to collapse and disperse (Trellis Bioscience). This dispersal renders the previously protected bacteria significantly more vulnerable to conventional antibiotics and host immune clearance, offering a promising approach to treating recalcitrant biofilm-mediated infections across a wide range of Gram-positive and Gram-negative species.
Sequestration and removal of DNABII proteins from the extracellular DNA (eDNA) scaffold within the biofilm matrix, leading to structural collapse and dispersal of the biofilm.
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