Minor fimbrial protein 1 (Mfa1) (Mfa1)

Minor fimbrial protein 1 (Mfa1) is a critical cell-surface adhesin of the periodontal pathogen Porphyromonas gingivalis (Daep et al., 2006, Infection and Immunity). It mediates the specific interspecies adherence between P. gingivalis and the commensal oral bacterium Streptococcus gordonii by binding to the SspB (Streptococcal surface protein B) protein (Demuth et al., 2001, Infection and Immunity). This interaction is a key early step in the colonization of the subgingival biofilm by P. gingivalis, which is a primary driver of chronic periodontitis (Hajishengallis et al., 2012, Nature Reviews Microbiology). The binding interface involves the recognition of a specific 27-amino acid sequence on SspB, known as the BAR (SspB Adherence Region) (Daep et al., 2008, Journal of Biological Chemistry). Therapeutic strategies targeting this interface, such as the BAR peptide or small-molecule inhibitors, aim to disrupt the incorporation of P. gingivalis into dental plaque. By preventing this attachment, these agents reduce the pathogen's ability to establish a niche and trigger the inflammatory destruction of periodontal tissues. Because this interaction is highly specific to the pathogen's integration into the biofilm, it represents a promising target for narrow-spectrum antimicrobial therapy that spares the healthy oral microbiome.

Other names

Minor fimbrial antigen 1Mfa1 adhesinPorphyromonas gingivalis minor fimbriaeMfa1 protein67 kDa fimbriae

Competitive inhibition of the Mfa1-SspB interaction to prevent Porphyromonas gingivalis colonization and biofilm integration.