Structure of C‐terminal fragment of Merozoite Surface Protein‐1 from Plasmodium vivax Determined by Homology Modelling and Molecular Dynamics Refinement

Abstract

One current vaccine candidate against Plasmodium vivax targeting asexual blood stage is the major merozoite surface protein- 1 of P. vivax (PvMSP-1). Vaccine trials with PvMSP-119 and PvMSP-133 have succeeded in protecting monkeys and a large proportion of individuals, naturally exposed to P. vivax transmission, develop specific antibodies to PvMSP-119. This study presents a model for the three-dimensional structure of the C-terminal 19 kDa fragment of P. vivax MSP-1 determined by means of homology modeling and molecular dynamics refinement. The structure proved to be consistent with MSP-119 of known crystal or solution structures. The presence of a main binding pocket, well suited for protein–protein interactions, was determined by CASTp. Corrections reported to the sequence of PvMSP-119 Belem strain were also inspected. Our model is currently used as a basis to understand antibody interactions with PvMSP-119.