Functional conservation of the malaria vaccine antigen MSP-119across distantly related Plasmodium species

1 January 2000

journal article
research article
Published by Springer Nature in Nature Medicine

Vol. 6 (1) , 91-95
https://doi.org/10.1038/71595

Abstract

The C-terminal region of Plasmodium falciparum merozoite surface protein 1 (MSP-1₁₉) is at present a leading malaria vaccine candidate. Antibodies against the epidermal growth factor-like domains of MSP-1₁₉are associated with immunity to P. falciparum^1,2,3,4 and active immunization with recombinant forms of the molecule protect against malaria challenge in various experimental systems^5,6,7,8. These findings, with the knowledge that epidermal growth factor-like domains in other molecules have essential binding functions, indicate the importance of this protein in merozoite invasion of red blood cells. Despite extensive molecular epidemiological investigations, only limited sequence polymorphism has been identified in P. falciparum MSP-1₁₉ (refs. 9, 10, 11). This indicates its sequence is functionally constrained, and is used in support of the use of MSP-1₁₉ as a vaccine. Here, we have successfully complemented the function of most of P. falciparum MSP-1₁₉ with the corresponding but highly divergent sequence from the rodent parasite P. chabaudi. The results indicate that the role of MSP-1₁₉ in red blood cell invasion is conserved across distantly related Plasmodium species and show that the sequence of P. falciparum MSP-1₁₉ is not constrained by function.

Keywords

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