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Structure of C-terminal fragment of merozoite surface protein-1 from Plasmodium vivax determined by homology modeling and molecular dynamics refinement |
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| Authors: | Serrano María Luisa Pérez Hilda A Medina J D |
| Institution: | aLaboratorio de Modelado Molecular, Unidad de Química Medicinal, Facultad de Farmacia, Universidad Central de Venezuela, Caracas 1041-A, Venezuela bLaboratorio de Inmunoparasitología, Centro de Microbiología y Biología Celular, IVIC, Apartado 21827, Caracas 1020-A, Venezuela cLaboratorio de Síntesis Orgánica y Productos Naturales, Centro de Química, IVIC, Apartado 21827, Caracas 1020-A, Venezuela |
| 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. |
| Keywords: | Homology modeling Molecular dynamics Malaria P vivax MSP-119 |
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