Bacteroides surface protein A (BspA) (BspA)

Bacteroides surface protein A (BspA) is a critical cell-surface virulence factor of the Gram-negative anaerobe Tannerella forsythia, a primary pathogen in chronic periodontitis [1][2]. Structurally, BspA is characterized by its leucine-rich repeat (LRR) motifs, which are essential for mediating protein-protein interactions and bacterial colonization [3]. The protein functions as a major adhesin, allowing the pathogen to bind to host epithelial cells and extracellular matrix components such as fibronectin and fibrinogen [2][4]. Crucially, BspA serves as a ligand for host Toll-like receptor 2 (TLR2), initiating a signaling cascade that leads to the overproduction of pro-inflammatory cytokines like IL-8 and TNF-alpha [4][5]. This localized inflammatory environment drives the destruction of periodontal connective tissue and alveolar bone loss [5]. Furthermore, BspA has been detected in atherosclerotic plaques, suggesting a role in systemic inflammatory diseases linked to oral infections [6]. While no targeted therapies are currently approved, BspA is a high-priority target for the development of vaccines and small-molecule inhibitors aimed at mitigating periodontal disease progression [1][5].

Other names

Tannerella forsythia BspALeucine-rich repeat protein BspABspA protein

Neutralization of bacterial adhesion and inhibition of TLR2-mediated inflammatory signaling.