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Plasmepsin V (PM-V) have functionally conserved orthologues across the  Plasmodium genus  who's binding and antigenic processing at the PEXEL motifs for export about 200–300 essential proteins is important for the virulence and viability of the causative  Plasmodium  species. This study was undertaken to determine  P. vivax  plasmepsin V Ind ( Pv PM-V-Ind) PEXEL motif export pathway for pathogenicity-related proteins/antigens export thereby altering  plasmodium  exportome during erythrocytic stages.    Method  We identify and characterize  Plasmodium vivax  plasmepsin-V-Ind (mutant) gene by cloning, sequence analysis, in  silico  bioinformatic protocols and structural modeling predictions based on docking studies on binding capacity with PEXEL motifs processing in terms of binding and accessibility of export proteins.    Results  Cloning and sequence analysis for genetic diversity demonstrates  Pv PM-V-Ind (mutant) gene is highly conserved among all isolates from different geographical regions of India. Imperfect duplicate insertion types of mutations (SVSE from 246–249 AA and SLSE from 266–269 AA) were identified among all Indian isolates in comparison to  P.vivax  Sal-1 ( Pv PM-V-Sal 1) isolate.  In silico  bioinformatics interaction studies of PEXEL peptide and active enzyme reveal that  Pv PM-V-Ind (mutant) is only active in endoplasmic reticulum lumen and membrane embedding is essential for activation of plasmepsin V. Structural modeling predictions based on docking studies with PEXEL motif show significant variation in substrate protein binding of these imperfect mutations with data mined PEXEL sequences. The predicted variation in the docking score and interacting amino acids of  Pv PM-V-Ind (mutant) proteins with PEXEL and lopinavir suggests a modulation in the activity of  Pv PM-V in terms of binding and accessibility at these sites.    Conclusion/Significance  Our functional modeled validation of  Pv PM-V-Ind (mutant) imperfect duplicate insertions with data mined PEXEL sequences leading to altered binding and substrate accessibility of the enzyme makes it a plausible target to investigate export mechanisms for  in silico  virtual screening and novel pharmacophore designing.

plos one

Imperfect Duplicate Insertions Type of Mutations in Plasmepsin V Modulates Binding Properties of PEXEL Motifs of Export Proteins in Indian Plasmodium vivax