Streptococcus pneumoniae binds collagens and C1q via the SSURE repeats of the PfbB adhesin.

ABSTRACT: The binding of Streptococcus pneumoniae to collagen is likely an important step in the pathogenesis of pneumococcal infections, but little is known of the underlying molecular mechanisms. Streptococcal surface repeats (SSURE) are highly conserved protein domains present in cell wall adhesins from different Streptococcus species. We find here that SSURE repeats of the pneumococcal adhesin plasminogen and fibronectin binding protein B (PfbB) bind to various types of collagen. Moreover, deletion of the pfbB gene resulted in a significant impairment of the ability of encapsulated or unencapsulated pneumococci to bind collagen. Notably, a PfbB SSURE domain is also bound to the complement component C1q that bears a collagen-like domain and promotes adherence of pneumococci to host cells by actin

SUBMITTER: De Gaetano GV 

PROVIDER: S-EPMC9328315 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature