Demonstration of a receptor for mouse and human serum albumin in Streptococcus pyogenes.

A new type of surface receptor for serum albumin was detected in strains of Streptococcus pyogenes (group A). This receptor, called type e, was different from albumin receptors in other streptococcal species. Only mouse and human serum albumin was bound to the receptor. The albumin-binding capacity was high: 2 X 10(8) bacterial organisms bound 11 micrograms of mouse albumin. The receptor was stable even when treated at 100 degrees C for 5 min. Binding of albumin was not mediated by lipoteichoic acid (LTA) because of lack of correlation to surface LTA, restricted albumin reactivity, and positive binding in presence of 2% Tween 20. Presence of albumin receptor type e correlated to presence of M-protein as measured by growth in the bactericidal test. All 51 M-protein positive group A streptococcal strains tested could bind mouse albumin whereas only 3 out of 8 M-protein negative strains showed positive binding (P less than 0.001). The sensitivity to trypsin digestion suggests that the albumin receptor is of protein nature or mediated by a protein.