PHOSPHORYLATION OF MYCOPLASMA-PNEUMONIAE CYTADHERENCE-ACCESSORY PROTEINS IN CELL-EXTRACTS

A cell-free system was used to characterize the phosphorylation of Myc oplasma pneumoniae proteins HMW1 acid HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infecti on. The pH and cation requirements for phosphorylation of HMW1 and HMW 2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibitors and stimulators on this process were examined. Phosphoamino acid analysis identified seri ne as the major phosphate acceptor for both HMW1 and HMW2 in this syst em.