Open AccessMembrane proteins with molecular masses of 88, 90 and 150 kDa are responsible for binding of human immunoglobulin G Fc fragment to the native cells of Mycoplasma salivarium
Author(s) -
Shibata Kenichiro,
Sawa Yoshihiko,
Inoue Satoshi,
Noda Mamoru,
Watanabe Tsuguo
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07239.x
Subject(s) - pronase , molecular mass , gel electrophoresis , antibody , microbiology and biotechnology , biochemistry , biology , polyclonal antibodies , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , mannose , immunoglobulin g , chemistry , trypsin , enzyme , immunology
Mycoplasma salivarium cells bound the Fc fragment of human immunoglobulin G. The activity was remarkablu enhanced by Mn + , but not by Mg 2+ and Ca 2+ ; significantly inhibited by d‐mannose; and reduced by pronase treatment of the cells. About 90% of the cells treated with pronase were not disrupted. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of proteins of the cells treated with pronase indicated that proteins with molecular masses of 88, 90 and 150 kDa (88 kp, 90 kp and 150 kp) were specifically digested. The results presented suggest that 88 kp, 90 kp and 150 kp, located in the outer surface of the cell membrane, are responsible for the activity of the M. salivarium cells and interact with a carbohydrate‐containing moiety (d‐mannose) of the Fc fragment in a Mn 2+ ‐dependent manner.