Intraerythrocytic malaria parasites degrade haemoglobin to provide nutrients for 
their own growth and maturation. Plasmodium aspartic proteases known as 
plasmepsins play an important role on haemoglobin degradation and are being 
studied as drug targets for chemotherapy of malaria. The rodent model for human 
malaria, Plasmodium chabaudi, is an experimentally good model for therapy drug 
design. The gene encoding an aspartic protease precursor (proplasmepsin) from 
the rodent malaria parasite P. chabaudi was cloned and sequenced. A theoretical 
3D structure model was constructed by comparative homology and used for 
superimposition with other known models. Analysis of the P. chabaudi and 
Plasmodium yoelli genomes revealed in both the presence of at least seven 
plasmepsins and each one has sequence similarity to its plasmepsin counterpart 
of the human malaria Plasmodium falciparum. The predicted proteins were 
confirmed as plasmepsins by detection on Blocks Database of three characteristic 
blocks of the eukaryotic and viral aspartic protease family. Analysis of the 
proline-rich loop amino acid sequence of these plasmepsins suggests that they 
constitute characteristic motifs of each plasmepsin group suggesting that these 
sequence variations are related with different substrate specificities.