Evidence for actinlike proteins in an M protein-negative strain of Streptococcus pyogenes

Abstract

Antigens shared between Streptococcus pyogenes and heart tissue may play an important role in autoimmune cardiac injury associated with acute rheumatic fever. Antiheart/antistreptococcal antibodies found in the disease react with antigens of S. pyogenes, including M protein and a 60-kDa antigen distinct from M protein. Heart antigens recognized by these cross-reactive antistreptococcal antibodies include myosin and actin. To investigate the presence of a streptococcal actin, established protocols for the polymerization and isolation of eukaryotic actin were used to extract and concentrate actinlike proteins from M- streptococcal cells. The polymerized bacterial actin from the streptococcal extract was probed in immunoblots with an antiactin monoclonal antibody. Two proteins of about 60 kDa in the polymerized bacterial actin reacted with the antiactin antibody. Proteins in the polymerized bacterial actin extract of about 43 and 60 kDa behaved like eukaryotic actin by binding to myosin and DNase I affinity columns. Filaments were demonstrated by electron microscopy in the polymerized bacterial actinlike extract, which also enhanced the ATPase activity of eukaryotic myosin. The data suggest that proteins resembling actin are present in S. pyogenes.