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Published on: August 5, 2021
Structure of C-terminal fragment of merozoite surface protein-1 from Plasmodium vivax determined by homology modeling
María Luisa Serrano1, Hilda A Pérez, J D Medina
1Laboratorio de Modelado Molecular, Unidad de Química Medicinal, Facultad de Farmacia, Universidad Central de Venezuela, Caracas 1041-A, Venezuela. serranol@ucv.ve
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-1(19) and PvMSP-1(33) have succeeded in protecting monkeys and a large proportion of individuals, naturally exposed to P. vivax transmission, develop specific antibodies to PvMSP-1(19). This study presents a model for the three-dimensional structure of the C-terminal 19kDa fragment of P. vivax MSP-1 determined by means of homology modeling and molecular dynamics refinement. The structure proved to be consistent with MSP-1(19) 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-1(19) Belem strain were also inspected. Our model is currently used as a basis to understand antibody interactions with PvMSP-1(19).
Insights
A 3D model of Plasmodium vivax major merozoite surface protein-1 (PvMSP-1) was created to understand antibody interactions. This vaccine target shows potential for malaria control, aiding future drug development.
Area of Science:
- Structural biology
- Parasitology
- Immunology
Background:
- Plasmodium vivax malaria remains a significant global health challenge.
- The asexual blood stage parasite antigen, P. vivax major merozoite surface protein-1 (PvMSP-1), is a key target for malaria vaccine development.
- Previous studies with PvMSP-1 fragments (PvMSP-1(19) and PvMSP-1(33)) have shown protective efficacy in animal models and antibody induction in naturally exposed humans.
Purpose of the Study:
- To generate a three-dimensional structural model of the C-terminal 19kDa fragment of P. vivax MSP-1 (PvMSP-1(19)).
- To analyze the structural features of PvMSP-1(19), including potential binding sites for antibody interactions.
- To provide a structural basis for understanding antibody recognition of PvMSP-1(19) and inform vaccine design.
Main Methods:
- Homology modeling was employed to predict the 3D structure of PvMSP-1(19).
- Molecular dynamics refinement was used to optimize the generated structural model.
- Computational analysis using CASTp identified potential protein-protein interaction sites, specifically binding pockets.
Main Results:
- A reliable 3D structural model of PvMSP-1(19) was successfully generated.
- The model's structural integrity was validated against known crystal and solution structures of MSP-1(19).
- A significant binding pocket, suitable for protein-protein interactions, was identified within the PvMSP-1(19) structure.
Conclusions:
- The developed 3D model of PvMSP-1(19) provides crucial insights into its structural characteristics.
- This model serves as a foundation for investigating antibody binding epitopes on PvMSP-1(19).
- The findings support the continued development of PvMSP-1 based vaccines for P. vivax malaria control.
