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Title: Biochemical and immunological characterization of E. coli expressed 42 kDa fragment of Plasmodium vivax and P. cynomolgi bastianelli merozoite surface protein-1
Authors: Kaushal, Deep C
Kaushal, Nuzhat A
Narula, Atul
Kumar, Niraj
Puri, S K
Dutta, Shitij
Lanar, David E
Keywords: Plasmodium vivax
Plasmodium cynomolgi
Merozoite surface protein-1
Rhesus monkey
Issue Date: Dec-2007
Publisher: CSIR
Abstract: Plasmodium vivax is one of the most widely distributed human malaria parasites and due to drug-resistant strains, its incidence and prevalence has increased, thus an effective vaccine against the parasites is urgently needed. One of the major constraints in developing P. vivax vaccine is the lack of suitable in vivo models for testing the protective efficacy of the vaccine. P. vivax and P. cynomolgi bastianelli are the two closely related malaria parasites and share a similar clinical course of infection in their respective hosts. The merozoite surface protein-1 (MSP-1) of these parasites has found to be protective in a wide range of host-parasite systems. P. vivax MSP-1 is synthesized as 200 kDa polypeptide and processed just prior to merozoite release from the erythrocytes into smaller fragments. The C- terminal 42 kDa cleavage product of MSP-1 (MSP-1₄₂) is present on the surface of merozoites and a major candidate for blood stage malaria vaccine. In the present study, we have biochemically and immunologically characterized the soluble and refolded 42 kDa fragment of MSP-1 of P. vivax (PvMSP-1₄₂) and P. cynomolgi B (PcMSP-1₄₂). SDS-PAGE analysis showed that both soluble and refolded E. coli expressed P. vivax and P. cynomolgi B MSP-1₄₂ proteins were homogenous in nature. The soluble and refolded MSP-1₄₂ antigens of both parasites showed high reactivity with protective monkey sera and conformation-specific monoclonal antibodies against P. cynomolgi B and P. vivax MSP-1₄₂ antigens. Immunization of BALB/c mice with these antigens resulted in the production of high titres of cross-reactive antibodies primarily against the conformational epitopes of MSP-1₄₂ protein. The immune sera from rhesus monkeys, immunized with soluble and refolded MSP-142 antigens of both parasites also showed high titered cross-reactive antibodies against MSP-1₄₂ conformational epitopes. These results suggested that the soluble and refolded forms of E. coli expressed P. vivax MSP-1₄₂ antigens were highly immunogenic and thus a viable candidate for vaccine studies.
Page(s): 429-436
ISSN: 0301-1208
Source:IJBB Vol.44(6) [December 2007]

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