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

Kim, Tong-Soo, Kim, Hyung-Hwan, Moon, Sung-Ung, Lee, Sun-Sim, Shin, E-Hyun, Oh, Chang-Mi, Kang, Yoon-Joong, Kim, Do-Kyung, Sohn, Youngjoo, Kim, Hyuck, Lee, Hyeong-Woo
Experimental parasitology 2011 v.127 no.2 pp. 346-350
Anopheles sinensis, Escherichia coli, Plasmodium vivax, amino acids, genes, immune response, longevity, malaria, mice, molecular weight, monoclonal antibodies, parasitology, patients, polyacrylamide gel electrophoresis, polymerase chain reaction, recombinant proteins, surface proteins, vaccines, Korean Peninsula
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 28kDa 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.