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      The role of Pvs28 in sporozoite development in Anopheles sinensis and its longevity in BALB/c mice.

      Experimental Parasitology
      Animals, Anopheles, parasitology, Antibodies, Monoclonal, biosynthesis, immunology, Antibodies, Protozoan, blood, Antigens, Protozoan, genetics, Antigens, Surface, Blotting, Western, Cloning, Molecular, Cytokines, DNA, Protozoan, chemistry, Female, Humans, Insect Vectors, Malaria Vaccines, Malaria, Vivax, prevention & control, transmission, Mice, Mice, Inbred BALB C, Plasmodium vivax, growth & development, Polymerase Chain Reaction, Recombinant Proteins

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          Abstract

          To develop a vivax malaria vaccine for blocking malarial transmission, the ookinete surface protein Pvs28 was cloned from Korean malaria patients using polymerase chain reaction. The Pvs28 gene consists of 726bp and encodes 241 amino acids. It was subcloned into the expression vector pQE30 and expressed in Escherichia coli. The expressed recombinant protein, rPvs28, has a molecular weight of about 28 kDa in SDS-PAGE analysis. A monoclonal antibody against rPvs28 was produced using BALB/c mice. It inhibited sporozoite development in Anopheles sinensis mosquitoes (n = 81) which is one of the malaria vectors in Korea, with relatively high antibody titer against rPv28 persisting for more than 6 months. These results indicate that rPvs28 induces an immune response in mice that effectively blocks sporozoite development in mosquitoes. Therefore it could be a vaccine candidate for preventing vivax malaria in Korea. Copyright © 2010 Elsevier Inc. All rights reserved.

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