Purification, Characterization, and Immunogenicity of a Disulfide Cross-Linked Plasmodium vivax Vaccine Candidate Antigen, Merozoite Surface Protein 1, Expressed in Escherichia coli (original) (raw)

2001, Infection and Immunity

AI-generated Abstract

Plasmodium vivax is a significant cause of malaria, accounting for a large proportion of cases in specific regions. The necessity for an effective vaccine has grown with the emergence of drug-resistant strains. Traditional methods have struggled to produce viable recombinant P. vivax antigens, primarily due to challenges in expressing proteins with complex structures in Escherichia coli. This study presents the expression of a candidate vaccine antigen, the merozoite surface protein 1 (PvMSP-1 p42), using a modified E. coli strain that supports disulfide bond formation, allowing for successful purification and characterization of the protein. Immunization studies indicate that PvMSP-1 p42 generates robust immune responses, suggesting its potential as a viable malaria vaccine candidate.

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