Several exported Plasmodium falciparum(Pf) proteins contribute to malaria biology through their involvement in cytoadherence, immune evasion and host cell remodelling. Many of these exported proteins and other host molecules are present in iRBC (infected red blood cell) generated extracellular vesicles (EVs), which are responsible for host cell modification and parasite development. CX3CL1 binding proteins (CBPs) present on the surface of iRBC have been reported to contribute to cytoadhesion by binding with the chemokine 'CX3CL1' via their extracellular domains. Here, we have characterized the cytoplasmic domain of CBP2to understand its function in parasite biology using biochemical and biophysical methods.Recombinant cytoplasmic CBP2 (rcCBP2) binds nucleic acids showing interaction with DNA/RNA. rcCBP2 shows dimer formation under non-reducing conditions highlighting the role of disulphide bonds in oligomerization while ATP binding leads to structural changes in the protein. In vitro interaction studies depict its binding with a Maurer's cleft resident protein 'PfSBP1', which is influenced by ATP binding of rcCBP2. Our results suggest CBP2 as a two-

Plasmodium falciparum is a causative agent of one of the most devastating disease, cerebral malaria. Absence of suitable vaccine and the emergence of multi drug resistant parasites hinder prevention of malaria disease worldwide. One of the most reliable approaches to control this disease is to develop antimalarial against drug targets which are specific for ubiquitous and necessary enzymes such as helicases. Helicases work in ATP dependent manner and help in unwinding of nucleic acids during replication, transcription and repair mechanism. In this study, in silico analysis and homology modeling method were used to characterize the physicochemical properties and 3D structure of PfBrr2 helicase. Suitable structure of different domains was validated using in silico tools and used for docking studies to understand protein-ligand interactions. Protein-protein interaction network of PfBrr2 was investigated to understand its function inside the parasite.

Abbreviations: ds-DNA, double stranded DNA; EC, endothelial cell; HRP, horse radish peroxidase; hr, hour; iRBC, infected red blood cell; MC, Maurer's cleft; NC, Nitrocellulose membrane; PfSBP1, Plasmodium falciparum skeleton binding protein-1; PfEMP1, Plasmodium falciparum erythrocyte membrane protein-1; PEXEL, Plasmodium export element; RNA, Ribonucleic acid; RBC, red blood cell; ss-DNA, single stranded DNA; TROVE, telomerase, Ro and vault module. Abstract: Several exported Plasmodium falciparum(Pf) proteins contribute to malaria biology through their involvement in cytoadherence, immune evasion and host cell remodelling. Many of these exported proteins and other host molecules are present in iRBC (infected red blood cell) generated extracellular vesicles (EVs), which are responsible for host cell modification and parasite development. CX3CL1 binding proteins (CBPs) present on the surface of iRBC have been reported to contribute to cytoadhesion by binding with the chemokine 'CX3CL1' via their extracellular domains. Here, we have characterized the cytoplasmic domain of CBP2to understand its function in parasite biology using biochemical and biophysical methods. Recombinant cytoplasmic CBP2 (rcCBP2) binds nucleic acids showing interaction with DNA/RNA. rcCBP2 shows dimer formation under non-reducing conditions highlighting the role of disulphide bonds in oligomerization while ATP binding leads to structural changes in the protein.In vitro interaction studies depict its binding with a Maurer's cleft resident protein 'PfSBP1', which is influenced by ATP binding of rcCBP2. Our results suggest CBP2 as a two-