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Expression, polymorphism analysis, reticulocyte binding and serological reactivity of twoPlasmodium vivaxMSP-1 protein recombinant fragments
Among the four parasite species causing malaria in humans,Plasmodium vivaxprevails on both the Asian and the American continents. Several antigens from this parasite's erythrocytic stages have been characterised and some of them are considered to be good vaccine candidates. TheP. vivaxmerozoite...
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Published in: | Vaccine 2003-03, Vol.21 (11-12), p.1033 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Among the four parasite species causing malaria in humans,Plasmodium vivaxprevails on both the Asian and the American continents. Several antigens from this parasite's erythrocytic stages have been characterised and some of them are considered to be good vaccine candidates. TheP. vivaxmerozoite surface protein-1 (PvMSP-1) is a 200kDa antigen, thought to mediate the initial contact between the merozoite and the erythrocyte. An effective blockage of this interaction could be important in anti-malarial vaccine design. This study analyses the genetic polymorphism, binding to both reticulocytes and erythrocytes, antigenicity and immunogenicity of two recombinant proteins belonging to the 33kDa PvMSP-1 proteolytic fragment. Both regions showed very low genetic variation, bound reticulocytes with higher affinity than erythrocytes, were recognised by naturallyP. vivax-infected patient sera and were immunogenic when used to immunise rabbits, making them good vaccine candidates againstP. vivax, to be further preclinically tested in theAotusmonkey model. |
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ISSN: | 0264-410X 1873-2518 |
DOI: | 10.1016/S0264-410X(02)00660-6 |