Phosphorylation of proteins in virulent promastigotes from Leishmania major.

Protein kinases are present in the plasma membrane of the human parasite Leishmania. A marked increase in enzyme activity has been detected as cultures entered into the stationary phase of growth. Since avirulent parasites can be separated from virulent forms by the peanut agglutinin (PNA), we have examined the change in the protein kinase activity of L. major during growth in vitro and the difference in phosphorylation with virulent promastigotes (PNA-) of L. major. Marked similarities were found between the phosphorylation patterns of the logarithmic and stationary phase promastigotes of L. major. On the other hand, when the phosphorylation pattern of those proteins, shared by both the metacyclic (PNA-) promastigotes and the stationary phase cells, was examined, a marked increase in both the total number of phosphoproteins and the extent of their phosphorylation was observed in PNA-. Both the increase in protein kinase activity in the stationary phase parasites and the marked changes in phosphorylation in the highly infective promastigotes, may provide a clue as to the adaptative mechanism which enable promastigotes to survive within the vertebrate host.