PREDICTION OF CRITICAL RESIDUES IN PFEMP1 USING INFORMATION THEORETIC MEASURES

Abstract

PfEMP1(Plasmodium falciparum erythrocyte membrane protein) is an important target for protective immunity and is implicated in the pathology of malaria through its ability to adhere to host endothelial receptors. PfEMP1 has specific domains which are important in its cytoadherence function. PfEMP1 binds to CD36, an 88 kDa glycoprotein found in several cell types including platelets, monocytes, dendritic cells, and micro vascular endothelial cells. This cytoadherence of PFEMP1 to CD36 receptor is due to a specific domain called CIDR1α domain. We hypothesize that the cytoadherence function of CIDR1α to CD36 receptor is facilitated by various conserved motifs which may be targeted to disrupt the parasite cytoadherence system. Indepth knowledge of structure and function of various conserved motifs of CIDR1α is necessary for effective drug design and vaccine designing. Herein, we will be employing computational approaches to predict fold and functionally critical residues of CIDR1α domain.For this, information theoretic scores which are variants of Relative Entropy will be calculated from Multiple Sequence Alignment (MSA) by considering distinct physico-chemical properties. The residues of CIDR1α with high RE and CRE will be predicted to be fold and functionally significant respectively.