Structure of C-terminal fragment of merozoite surface protein-1 from Plasmodium vivax determined by homology modeling and molecular dynamics refinement

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.

The C-terminal merozoite surface protein-1 from Plasmodium vivax was determined by a combined use of various molecular modeling techniques. The main binding pocket was determined by CASTp. Corrections reported to the sequence of PvMSP-119 Belem strain were also inspected.Figure optionsDownload as PowerPoint slide