Immunoglobulin G Fc fragment-binding proteins in Mycoplasma salivarium cells.
Cell proteins of Mycoplasma salivarium were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to membranes, then examined for reactivity with human IgG molecules, the Fc fragment of human IgG, and concanavalin A (ConA). Multiple protein bands bound IgG, and most of them also bound ConA. One (corresponding to a molecular mass of 90 kDa) of the IgG- and ConA-binding bands intensely interacted with the Fc fragment of IgG. The reactivity of proteins eluted from the band with the Fc fragment, tested by dot-blotting and ELISA, was inhibited (90%) by pre-incubation with IgG and to a lesser extent (50%), with IgM. Thus, M. salivarium contained a cellular protein with a molecular mass of 90 kDa, that bound the Fc fragment of human IgG.
Sawa
Y
Y
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
Watanabe
T
T
Shibata
K
K
D001426:Bacterial Proteins / Q000276:immunology*; D003208:Concanavalin A; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D015151:Immunoblotting; D007141:Immunoglobulin Fc Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D007075:Immunoglobulin M / Q000276:immunology; D008970:Molecular Weight; D009174:Mycoplasma / Q000276:immunology*; D011961:Receptors, Fc / Q000276:immunology
D001426:Bacterial Proteins; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D011961:Receptors, Fc; D003208:Concanavalin A