MOUSE ANTI-PLASMODIUM VIVAX MSP1 ANTIBODY (PVM-1)

Mouse anti Plasmodium vivax MSP1 antibody (clone PVM-1) recognises major merozoite surface protein 1 (MSP1) from Plasmodium vivax. The antibody is suitable for ELISA and Western blot applications.

PRODUCT DETAILS – MOUSE ANTI-PLASMODIUM VIVAX MSP1 ANTIBODY (PVM-1)</2>

• Mouse Anti Plasmodium vivax MSP1 (IgG1, clone PVM-1) monoclonal antibody.
• Recognises Plasmodium vivax major merozoite surface protein 1 (MSP1).
• Suitable for use in ELISA and Western blot applications.
• Purified by Protein G Sepharose chromatography.
• Presented in phosphate buffered saline, pH 7.4 with 0.09% sodium azide.

BACKGROUND

Malaria is a globally widespread infectious disease caused by obligate intracellular protozoan parasites of the genus Plasmodium. Five different species of Plasmodium are known to cause disease in humans including P. falciparum, P. vivax, P. ovale, P. malariae and P. knowlesi. Most cases of Malaria occur in African regions and the Americas. In African regions, P. falciparum causes the majority of malaria cases, whereas P. vivax is the predominant cause of malaria in regions of the Americas (WHO).

Merozoite surface antigen is a protein located on the outside of the merozoite, which is an early life cycle stage of Plasmodium. During the asexual blood stage of its life cycle, the malaria parasite enters red blood cells to replicate itself, causing the classic symptoms of malaria. The MSP surface protein complexes are involved in multiple interactions of Plasmodium with the red blood cells (Kadekoppala and Holder, 2010). Merozoite surface proteins 1 and 2 (MSP1 & MSP2) are the most abundant (GPI)-anchored proteins on the surface of Plasmodium merozoites. The function of the MSP2 complex is not clear, but current research suggests it has a role in red blood cell invasion due to its degradation shortly after invasion (Beeson et al., 2016). MSP1 is synthesized at the very beginning of schizogony, or asexual merozoite reproduction. The merozoite first attaches to a red blood cell using its MSP1 complex which then targets spectrin, a complex on the internal surface of the cell membrane of a red blood cell. The majority of the MSP1 complex is shed upon entry into the red blood cell, but a small portion of the C-terminus, called MSP-119, is conserved. The exact role of MSP-119 remains unknown, but it currently serves as a marker for the formation of the food vacuole (Blackman et al., 1990).

MSPs have been a major target for vaccine development, with the aim of disrupting the merozoite at different stages in its life cycle. Those that target the merozoite in its asexual erythrocytic stage have utilized merozoite surface proteins, particularly MSP1 (Versiani et al., 2013). Other drugs have been developed which bind to MSPs in order to disrupt merozoite replication. However, the sequences encoding proteins such as MSP1 vary greatly depending on the region they are found, making them challenging targets.

REFERENCES

• Beeson et al (2016). Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria. FEMS Microbiol Rev. 40(3): 343–372.
• Kadekoppala and Holder (2010). Merozoite surface proteins of the malaria parasite: The MSP1 complex and the MSP7 family. International Journal for Parasitology. Volume 40, Issue 10, Pages 1155-1161.
• Blackman et al. (1990). A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion- inhibiting antibodies. J Exp Med. 172(1): 379–382.
• Versiani et al. (2013). N-Terminal Plasmodium vivax Merozoite Surface Protein-1, a Potential Subunit for Malaria Vivax Vaccine. Clin Dev Immunol. 2013: 965841.
• World Health Organization: Malaria. Key facts.