DNABII family DNA-binding protein (DNABII)

The DNABII family DNA-binding protein consists of integration host factor (IHF) and histone-like protein (HU), which are highly conserved bacterial proteins that bind DNA as dimers and condense it, playing essential roles in nucleoid structure and extracellular matrix stability. In bacterial biofilms, these proteins localize at vertices of the extracellular DNA (eDNA) lattice, stabilizing the interwoven web-like structure critical for biofilm integrity across pathogens like uropathogenic Escherichia coli (UPEC), nontypeable Haemophilus influenzae (NTHI), and Staphylococcus epidermidis. This stabilization protects bacteria from antibiotics and host immune responses, contributing to chronic and recurrent infections such as urinary tract infections, otitis media, and cystic fibrosis exacerbations. DNABII proteins exhibit high affinity for branched DNA structures like Holliday junctions, enabling them to act as lynchpins in the biofilm matrix. Targeting DNABII proteins with antibodies or inhibitors disrupts biofilm formation, promotes dispersal, and increases bacterial susceptibility to conventional antibiotics, positioning them as promising therapeutic targets for biofilm-mediated diseases. Experimental depletion of DNABII via anti-IHF antibodies reduces biofilm biomass and mechanical rigidity, while functional replacement with other Holliday junction-binding proteins like RuvA confirms their specific structural role.

Other names

integration host factor (IHF)histone-like protein (HU)HU protein

Disruption of biofilm extracellular matrix via antibody-mediated depletion or inhibitors targeting DNABII proteins to destabilize eDNA lattice and enhance antibiotic susceptibility