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• W2915068676 abstract "Malaria is an infectious disease that causes considerable mortality and morbidityglobally each year. The Merozoite Surface Protein-3 (MSP-3) is a multigene family ofproteins that is found on the surface of the Plasmodium merozoite. Multiple paralogs ofthe gene can be found in Plasmodium parasites and orthologs of this gene have also beenidentified in many different species of Plasmodium including P. knowlesi.In this study, 23 P. knowlesi clinical isolates were studied to evaluate geneticdiversity, polymorphisms and natural selection acting on the P. knowlesi MSP-3 (pkmsp3)gene. The pkmsp3 gene which contains a signal peptide, an alanine rich central domaindenoted Domain A, and a C-terminal region denoted Domain B was amplified by PCR,cloned into Escherichia coli and sequenced. A total of 48 pkmsp3 sequences wereobtained. The nucleotide diversity (π) of the full length sequence was found to bemarginally higher relative to other P. knowlesi functional genes. Diversity was found tobe higher for Domain A (π: 0.035 ± 0.012) and lower in Domain B (π: 0.028 ± 0.002).Comparisons and analysis with P. knowlesi strain H as a reference sequence showedmutations at 339 positions and these amino acid sequences could be categorised into 42haplotypes.Analysis of the phylogenetic tree and haplotype network revealed that thehaplotypes clustered and split into two main distinct groups. The Tajima’s D, Fu & Li’sD* and F* tests and codon based Z-test showed no significant departure from neutralityhowever, estimations of the dN/dS ratio for Domain B was 0.6, indicating that thisparticular domain may be under purifying selection.The pkmsp3 gene was then expressed as a ~34 kDa recombinant protein pkMSP-3 using an E. coli expression system. The sensitivity and specificity of the purifiedproteins were evaluated in Western Blot and ELISA. In Western Blot, pkMSP-3 exhibiteda sensitivity of 61.0% and a specificity of 100.0%. In ELISA, the pkMSP-3 protein wasivfound to have a sensitivity of 100.0% and a specificity of 97.1%. High sensitivity inELISA and high specificity in Western Blot indicates that this protein holds potential asan immunodiagnostic marker if both assays are used in tandem for diagnosis.This study then further aimed to evaluate the immunogenicity of pkMSP-3 usinga mouse model to evaluate if it had any potential to inhibit P. knowlesi merozoite invasioninto human normocytes. Mice were immunized with pkMSP-3 and displayedsignificantly higher levels of the cytokine interferon-gamma, interleukin-2 andinterleukin-6 when compared to cytokine levels in negative control mice. The pkMSP-3raised antibodies were found to have a high endpoint titre with IgG1 having the highestisotype distribution followed by IgG2b, IgG2a, IgG3 and finally IgG2c. The localizationof pkMSP-3-immunized mice antibodies was studied by immunofluorescencemicroscopy where the antibodies were found to localize around the membrane ofindividual merozoites. Lastly, a merozoite invasion assay was carried out using humannormocytes treated with or without pkMSP-3 monoclonal antibody. Human normocytestreated with pkMSP-3 monoclonal antibodies had a percent inhibition of 49.6% whereinvasion rates were almost halved compared to untreated human normocytes." @default.
• W2915068676 created "2019-02-21" @default.
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• W2915068676 date "2017-01-01" @default.
• W2915068676 modified "2023-09-23" @default.
• W2915068676 title "Genetic diversity study, expression and immunocharacterization of Plasmodium knowlesi merozoite surface protein-3 (MSP-3) in Escherichia /Jeremy Ryan De Silva" @default.
• W2915068676 hasPublicationYear "2017" @default.
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