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VOL. 72 (4), 629-642, 2006 PROTEIN PROCESSING IN PLASMODIUM FALCIPARUM?

expected size of the G6PD domain. In addition, in the mature stages
two other smaller bands were also detected: a 44 kDa band detected
with the anti-6PGL domain and a 39 kDa band detected with the
anti-G6PD domain, which could result from degradation of their
corresponding 73 kDa and 69 kDa band, respectively.

FIGURE 2. G6PD-6PGL protein patterns across the intraerythrocytic cycle of
P. falciparum. Expression patterns at protein level were examined through

immunodetection of the parasite G6PD-6PGL. Parasites harvested at the three
main stages, rings (R), trophozoites (T) and Schizonts (S) were transferred and
immunodeveloped with three different conditions using anti-6PGL domain, anti-

G6PD domain, and a mixture of both of them.

dsRNA silencing of the PfG6PD-6PGL and expression pattern

In an attempt at silencing the G6PD-6PGL gene, erythrocytes
infected with ring-stage P. falciparum 3D7 (pyrimethamine-sensitive
clone) were electroporated with a dsRNA-G6PD duplex, RNase-free
water and dsRNA-Rab5a (the last two as controls) as previously
reported (18).

The G6PD-6PGL protein band pattern during the P. falciparum
intraerythrocyte cycle, as revealed by immunodetection with both
antibodies is shown in Figure 3A. In all stages, two main bands
of different molecular weight were observed, a 107 kDa band

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