Streptococcal surface protein B (SspB) (SspB)

Streptococcal surface protein B (SspB) is a large surface-anchored protein belonging to the Antigen I/II family, primarily expressed by the oral commensal Streptococcus gordonii (Demuth et al., 2001, PubMed: 11157331). It plays a pivotal role in the development of dental plaque by acting as a receptor for Porphyromonas gingivalis, a keystone pathogen in periodontitis (Hajishengallis et al., 2012, PubMed: 22425126). The interaction is specifically mediated by the binding of P. gingivalis minor fimbriae (Mfa1) to a 27-residue motif on SspB known as the SspB Adherence Region or BAR (Daep et al., 2006, PubMed: 16790470). This adherence is a prerequisite for P. gingivalis colonization and its subsequent role in triggering inflammatory bone loss and tissue destruction. Therapeutic interventions targeting SspB, such as synthetic BAR peptides, have shown efficacy in inhibiting P. gingivalis recruitment into biofilms in vitro and in vivo (Daep et al., 2011, PubMed: 21402766). By selectively blocking this interspecies interaction, researchers aim to prevent periodontal disease while minimizing the impact on the beneficial oral microbiota.

Other names

Antigen I/IIAgI/IISspA/BBAR (SspB Adherence Region)Streptococcal adhesin

Competitive inhibition of the binding between Porphyromonas gingivalis Mfa1 fimbriae and the BAR domain of Streptococcus gordonii SspB protein.