Developmentally regulated expression of a novel 59-kDa product of the major surface protease (Msp or gp63) gene family of Leishmania chagasi.

All species of Leishmania express a major surface protease (Msp or gp63) that facilitates the interactions of the parasite with its environment at several steps in its life cycle. The msp gene family in Leishmania chagasi contains three classes of genes whose mRNAs are differentially expressed during parasite growth. Logarithmic phase (low infectivity) promastigotes express only 63-kDa versions of Msp, whereas stationary phase (high infectivity) promastigotes express both 63- and 59-kDa Msps. The different migrations of the 59- and 63-kDa proteins on acrylamide gels are not due to differences in N-linked glycosylation or the membrane anchor. Plasmid transfections of Leishmania demonstrate that mspS2 of the stationary gene class encodes a 59-kDa protein. Expression of the 59-kDa protein in stationary phase promastigotes ceases after about 12 weeks of in vitro cultivation when the parasites become attenuated. Attenuated parasites can be stimulated to re-express the 59-kDa Msp by passage through mice followed by several in vitro passages of recovered promastigotes. Amastigotes express yet another subset of Msp proteins. Thus, the 59-kDa product of mspS2 is expressed only in stationary phase promastigotes and only after recent exposure to environmental changes encountered in the mammalian host cell.