Bioinformatics analysis of the structure and function of NADPH-cytochrome p450 reductase of Plasmodium vivax.

The structure of NADPH-cytochrome p450 reductase (CPR) of Plasmodium falciparum (P. falciparum or Pf) has been determined using bioinformatics analysis. However, that of Plasmodium vivax (P. vivax or Pv) has not yet been determined. This study aimed to analyze the structure and function of PvCPR using bioinformatics analysis. The results demonstrated that PvCPR was an unstable and alkaline enzyme located in the cytoplasm of parasites with a signal peptide. It possessed seven types of signal sites and eight protein-protein binding sites, and had a tertiary structure resembling a forceps with a single wing, which differed from that of PfCPR. It also had nine linear B-cell epitopes and 10 antigenicity sites, which were not homologous with the amino acid sequence of Homo sapiens (H. sapiens or Hs) CPR and six fragments that were similar to fragments of immune-related protein sequences from H. sapiens. Therefore, the function of PvCPR may be different from that of PfCPR, and PvCPR may participate in the immune escape of P. vivax.