Interactions between membrane-bound streptococcal alpha-enolase and human plasminogen captured through cryogenic-electron microscopy.

ABSTRACT: Certain invasive strains of the Gram-positive bacterium Streptococcus pyogenes exploit human plasminogen (hPg) to promote tissue invasion and pathogenesis. hPg is a single-chain multi-modular zymogen containing five kringle domains (K1-K5), four of which interact with lysine or pseudo-lysine residues on binding partners, positioning hPg for activation to plasmin and enhancing bacterial dissemination. The major hPg binding protein in S. pyogenes is the multicopy surface-resident M-protein, or other surface proteins, such as the homooctameric glycolytic enzyme, enolase (SEn). SEn lacks features for direct translocation from the cytoplasm to the bacterial surface, and it is unclear how Sen is translocated to the bacterial surface. Additionally, the mechanism by which SEn binds h

SUBMITTER: Tjia-Fleck S 

PROVIDER: S-EPMC12504095 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature