Localization and stage specific phosphorylation of Plasmodium falciparum phosphoproteins during the intraerythrocytic cycle

An 88‐kDa protein of Plastmidium falciparum is related to the band‐3‐binding domain of human erythrocyte ankyrin

“…falciparum was used for all experiments. Parasite culture conditions, as well as isolation and lysis of the parasites, have been described previously (Suetterlin et al, 1991).…”

“…Proteins were phosphorylated with [32P]orthophosphate as reported by Suetterlin et al (1991). To screen for additional post-trans-lational modifications, unsynchronized parasite cultures of about 10% parasitemia were examined by 18 h incubations in RPMI complete media with either 0.1 Cijl [9, lO(n) …”

“…This event seems to be associated with intracellular growth of the parasite. In addition, there exist several further phosphoproteins which associate specifically with the membrane of infected erythrocytes (Suetterlin et al, 1991). The situation is more complicated in the case of Plasmodium berghei, where a minority of the infected erythrocytes filter in a manner similar to that of uninfected erythrocytes during all stages of parasite maturation (Pattanakitsakul and Yuthavong, 1982).…”

“…We recently described a pair of phosphoproteins with a molecular mass of about 88 kDa from P. falciparum (pf88-1 and pB8-2) (Suetterlin et al, 1991). These proteins are present in both the cytosolic and particulate fractions of the parasite, as well as in the membrane of infected erythrocytes during the entire erythrocytic growth cycle.…”

PfKIN, an SNF1 type protein kinase of Plasmodium falciparum predominantly expressed in gametocytes

“…The mammalian SNF1 homologue is the AMPactivated protein kinase which is known to play a central role in the regulation of lipid metabolism [9] and in cell response to stress [10] Plasmodium falciparum is a protozoan parasite responsible for the most severe form of human malaria. Although phosphorylation and dephos phorylation mechanisms are reported as playing an important role during merozoite invasion [12] as well as during intraerythrocytic development [13], relatively little is known about reversible phosphorylation during the parasite life cycle but it is reasonable to assume that these processes should regulate many aspects of the parasite life both in the vertebrate and invertebrate hosts, and during the transition phases from one host to the other. The identification and characterization of The PfKIN-deduced protein sequence contains all the characteristic sequence motifs of the eu karyotic protein kinases, some of these being in volved in ATP-binding, substrate recognition or catalysis.…”