Using bioinformatics and biochemical methods in the recent past we have reported the isolation and characterization of the main components of translation initiation complex eIF4F from malaria parasite Plasmodium falciparum. We reported that eukaryotic initiation factor 4A (eIF4A), eukaryotic initiation factor 4E (eIF4E), eukaryotic initiation factor 4G (eIF4G) and poly (A) binding protein (PABP) are structurally and functionally conserved in this parasite. In the present study we report further characterization of PfeIF4A and PfeIF4E. We report that PfeIF4A and PfeIF4E are co-localized and predominantly localized in the cytoplasm. The parasite cultures treated with co-addition of PfeIF4A and PfeIF4E double stranded RNA showed ∼67% growth inhibition suggesting that inhibition of two components of the same pathway is more effective for inhibiting the proliferation of the malaria parasite Plasmodium falciparum. These observations suggest that PfeIF4A and PfeIF4E are critical for parasite growth and survival.