Expression and in silico Analysis of CIDR?1 Recombinant Protein from Plasmodium Falciparum as a Malaria Subunit Vaccine Candidate

Malaria vaccination is an essential approach to combat malaria. One major protein studied for vaccine development Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP1). It contains several important domains malaria pathogenesis. The binding of Cysteine-rich interdomain region ?1 (CIDR?1) PfEMP1 endothelial C receptor (EPCR) associated with cerebral malaria, while CIDR?1 CD36 has been correlated uncomplicated vital function makes it a potential candidate prevent clinical features A long journey can be shortened by the advancement bioinformatics and biotechnology techniques. This study aimed express recombinant investigate its potency as subunit in silico analysis. Constructed CIDR?1-PfEMP1 was expressed E. coli BL21(DE3) after induction Isopropyl ß-D-1-thiogalactopyranoside (IPTG) purified using Ni-NTA column. In analysis on sequence conducted ProtParam Tool physicochemical properties, Iterative Threading ASSEmbly Refinement (I-TASSER) server JPred4 program predict secondary structure, 3D modelling, ligand-binding site, BepiPred 2.0 Kolaskar-Tangaonkar B-cell epitope, NetCTL determine T-cell Vaxijen v2.0 antigenicity. chimeric had 27 kDa molecular weight classified stable protein. structure consisted 6 helices connected loops. revealed similarity CD36-binding protein, EPCR-binding domain, involved rosetting. modelling demonstrated conserved sites accessible surface area, which are binding. epitopes non-allergenic. properties CIDR? indicated candidate. HIGHLIGHTS capacity showed rosetting, non-allergenic analysis, indicating GRAPHICAL ABSTRACT