Malaria causes a worldwide annual mortality of about a million people. Rapidly 
evolving drug-resistant species of the parasite have created a pressing need for 
the identification of new drug targets and vaccine candidates. By developing 
fractionation protocols to enrich parasites from low-parasitemia patient 
samples, we have carried out the first ever proteomics analysis of clinical 
isolates of early stages of Plasmodium falciparum (Pf) and P. vivax. 
Patient-derived malarial parasites were directly processed and analyzed using 
shotgun proteomics approach using high-sensitivity MS for protein 
identification. Our study revealed about 100 parasite-coded gene products that 
included many known drug targets such as Pf hypoxanthine guanine phosphoribosyl 
transferase, Pf L-lactate dehydrogenase, and Plasmepsins. In addition, our study 
reports the expression of several parasite proteins in clinical ring stages that 
have never been reported in the ring stages of the laboratory-cultivated 
parasite strain. This proof-of-principle study represents a noteworthy step 
forward in our understanding of pathways elaborated by the parasite within the 
malaria patient and will pave the way towards identification of new drug and 
vaccine targets that can aid malaria therapy.