Functional conservation of the malaria vaccine antigen MSP-1(19) across distantly related Plasmodium species
- Author(s)
- O'Donnell, RA; Saul, A; Cowman, AF; Crabb, BS;
- Details
- Publication Year 2000-01,Volume 6,Issue #1,Page 91-95
- Journal Title
- NATURE MEDICINE
- Publication Type
- Journal Article
- Abstract
- The C-terminal region of Plasmodium falciparum merozoite surface protein 1 (MSP-1(19)) is at present a leading malaria vaccine candidate. Antibodies against the epidermal growth factor-like domains of MSP-1(19) are associated with immunity to P. falciparum(1-4) and active immunization with recombinant forms of the molecule protect against malaria challenge in various experimental systems(5-8), 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-1(19) (refs, 9-11). This indicates its sequence is functionally constrained, and is used in support of the use of MSP-1(19) as a vaccine. Here, we have successfully complemented the function of most of P. falciparum MSP-1(19) with the corresponding but highly divergent sequence from the rodent parasite P. chabaudi. The results indicate that the role of MSP-1(19) in red blood cell invasion is conserved across distantly related Plasmodium species and show that the sequence of P. falciparum MSP-1(19) is not constrained by function.
- Publisher
- NATURE AMERICA INC
- Keywords
- MEROZOITE SURFACE PROTEIN-1; TERMINAL FRAGMENT; SERUM ANTIBODIES; FALCIPARUM; INVASION; EPITOPES; INHIBIT; REGION; CELL
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- Refer to copyright notice on published article.
Creation Date: 2000-01-01 12:00:00