Novel complex formed between a nonproteolytic cell wall protein of group A streptococci and alpha 2-macroglobulin.
Binding of 125I-labeled alpha 2-macroglobulin (alpha 2M) to streptococci belonging to serological groups A, B, C, and G was studied. Streptococci of groups A and G interacted only with native alpha 2M, and those of group C reacted only with alpha 2M-trypsin complex. Binding of alpha 2M to group A streptococci was saturable and reversible. The dissociation constant was 2.02 X 10(-7) M, and the number of binding sites was calculated to be 18,000 per streptococcus. The alpha 2M-binding protein could be solubilized by treatment of group A streptococci with a murolytic enzyme and subsequently purified by affinity chromatography and high-pressure liquid chromatography. The purified protein was homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had a molecular weight of 78,000. It possessed no proteolytic activity and interacted with native alpha 2M in Western blots (immunoblots). Interaction of purified binding protein with alpha 2M led to a change in the conformation of alpha 2M similar to that obtained by alpha 2M-protease complexes. Reversible binding of a nonproteolytic streptococcal component of alpha 2M is thus a novel feature of alpha 2M reactivity.
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D008970:Molecular Weight; D011487:Protein Conformation; D013291:Streptococcus / Q000378:metabolism; D013292:Streptococcus agalactiae / Q000378:metabolism; D013297:Streptococcus pyogenes / Q000378:metabolism*; D000511:alpha-Macroglobulins / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; C053325:alpha 2-macroglobulin-binding protein, streptococci; D000511:alpha-Macroglobulins