Albumin-binding proteins on the surface of the Streptococcus milleri group and characterization of the albumin receptor of Streptococcus intermedius C5.

Abstract

Members of the Streptococcus milleri group (SMG) that react with Lancefield group C antisera were shown to bind large amounts of albumin although there was no direct relation between these two properties as polyclonal antisera to Lancefield group C antigen did not prevent the binding of albumin. There was a specificity for albumin binding, with albumin from man, monkeys, cat, dog and mouse being bound to a greater degree than albumin from cow, horse, goat or rabbit. Gold-labelled albumin was shown to be located close to the surface of strains by transmission electron microscopy. A cell-surface protein of M(r) 24,000, which was liberated by lysozyme treatment of cells, was shown to be the cell-surface receptor on Streptococcus intermedius C5. The receptor was physically dissimilar from protein G, an albumin- and IgG-binding protein of 'large-colony' Lancefield group C and G streptococci.