Ciliostatic, hemagglutinating, and proteolytic activities in a cell extract of Mycoplasma pneumoniae.
An extract of Mycoplasma pneumoniae, prepared from glass-grown organisms by extraction with 2 M NaCl, followed by freeze-thaw, ultracentrifugation, dialysis, and lyophilization, yielded approximately 20% of the total mycoplasmal protein. The extract contained at least 20 protein bands on sodium dodecyl sulfate-polyacrylamide gels and 2 to 5% carbohydrate and inhibited 70 to 100% of the ciliary activity of hamster tracheal organ cultures (ciliostasis). The extent of ciliostasis was dependent on the concentration of the extract. The extract also produced hemagglutination of human O-positive erythrocytes and showed proteolytic activity with a synthetic tetrapeptide substrate, S-2222. These in vitro tissue-damaging activities may be associated with the virulence of the mycoplasmas and with the pathogenesis of M. pneumoniae disease.
D000818:Animals; D002863:Chromogenic Compounds; D002923:Cilia; D006224:Cricetinae; D006384:Hemagglutination; D006801:Humans; D009177:Mycoplasma pneumoniae; D010447:Peptide Hydrolases; D011019:Pneumonia, Mycoplasma / Q000209:etiology; D014774:Virulence
D002863:Chromogenic Compounds; D010447:Peptide Hydrolases