Hemagglutination activity and localization of Fc receptor of group A and G streptococci.
The IgG-Fc binding activity and binding sites on the cell surface of streptococci, strains AR1 (group A) and G148 (group G), and Staphylococcus aureus strain Cowan I were examined by hemagglutination (HA) and immunoelectron microscopic methods. No distinct difference was observed in the HA activity among these three strains. However, the strains differed in the distribution of Fc receptor. Cowan I cells (having protein A) were heavily covered with two layers of ferritin particles, whereas AR1 cells were heavily covered with a single, rough layer of ferritin particles. G148 cells (having protein G) were labeled with a relatively thin, rough ferritin layer. The trypsin susceptibility of the Fc receptors of the AR1 strain was much higher than that of the G148 strain. These results suggest that both streptococcal strains are distinctly different in the arrangement or in the conformation of the Fc receptor from the Cowan I strain. It is also suggested that the Fc receptor molecules of the streptococcal strains differ from each other not only in conformation but also in trypsin susceptibility.
Yamada
S
S
Department of Microbiology, Kawasaki Medical School, Okayama.
Matsumoto
A
A
D006384:Hemagglutination; D007074:Immunoglobulin G / Q000276:immunology; D008854:Microscopy, Electron; D011961:Receptors, Fc / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D013211:Staphylococcus aureus / Q000032:analysis / Q000276:immunology / Q000648:ultrastructure; D013291:Streptococcus / Q000032:analysis / Q000276:immunology* / Q000648:ultrastructure; D013297:Streptococcus pyogenes / Q000032:analysis / Q000276:immunology / Q000648:ultrastructure; D014357:Trypsin / Q000378:metabolism
D007074:Immunoglobulin G; D011961:Receptors, Fc; D014357:Trypsin