Gardnerella vaginalis adhesion sites and biofilm matrix components

Gardnerella vaginalis adhesion sites and biofilm matrix components represent a multifaceted set of targets essential for the pathogenesis of Bacterial Vaginosis (BV). The initial colonization of the vaginal epithelium is facilitated by various adhesins, such as the pore-forming toxin vaginolysin (VLY), which targets host CD59 (Morrill et al., 2023), and sialidases (e.g., NanH) that degrade the protective mucus layer and expose glycan receptors (Lewis et al., 2013). Other structural components, including Tad pili and Cna-like proteins, further stabilize the attachment of the bacteria to host tissues (Pathogens, 2021; NIH, 2025). Once established, G. vaginalis coordinates the assembly of a dense biofilm matrix composed of extracellular DNA (eDNA), proteins, and exopolysaccharides like N-acetylglucosamine (NIH, 2011; NIH, 2024). This matrix acts as a protective shield, significantly increasing the bacteria's tolerance to the host immune response and conventional antibiotics such as metronidazole (PLOS, 2026). Therapeutic strategies under investigation focus on disrupting this matrix using enzymes like DNase and proteases, or preventing adhesion to reduce the likelihood of chronic and recurrent infections (NIH, 2011; NIH, 2024). Understanding these components is vital for developing more effective treatments that can eradicate persistent biofilms while sparing the beneficial vaginal microbiota (J Appl Microbiol, 2026).

Other names

Gardnerella vaginalis biofilmGV biofilm matrixGardnerella adhesinsBacterial Vaginosis biofilm matrixGardnerella virulence factors

Drugs targeting these components act through various mechanisms, including the inhibition of bacterial nucleic acid and protein synthesis (e.g., metronidazole, clindamycin), enzymatic degradation of the biofilm's structural eDNA and protein scaffold (e.g., DNase, proteases), and physical disruption of the matrix using surfactants or antiseptics (e.g., sodium cocoamphoacetate, boric acid).