Inhibition of Fibrinolysis by Streptococcal Phage Lysin_SM1.

ABSTRACT: Expression of bacteriophage lysin_SM1 by Streptococcus oralis strain SF100 is thought to be important for the pathogenesis of infective endocarditis, due to its ability to mediate bacterial binding to fibrinogen. To better define the lysin_SM1 binding site on fibrinogen Aα, and to investigate the impact of binding on fibrinolysis, we examined the interaction of lysin_SM1 with a series of recombinant fibrinogen Aα variants. These studies revealed that lysin_SM1 binds the C-terminal region of fibrinogen Aα spanned by amino acid residues 534 to 610, with an affinity of equilibrium dissociation constant (K_D) of 3.23 × 10^-5 M. This binding site overlaps the known binding site for plasminogen, an inactive precursor of plasmin,

SUBMITTER: Ji HJ 

PROVIDER: S-EPMC8263008 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature