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PubMedDate not supplied

Plasmodium lactate dehydrogenase assay to detect malarial parasites.

BACKGROUND: Microscopic examination of blood smears remains the gold standard for the diagnosis of malaria. However, it is labour-intensive and requires skilled operators. Immunochromatographic dipstick assays provide a potential alternative. One such dipstick, the Plasmodium lactate dehydrogenase assay (pLDH), is based on detection of the Plasmodium intracellular metabolic enzyme, LDH. The differentiation of malarial parasites is based on the antigenic differences between the pLDH isoforms. This study was designed to assess the sensitivity and specificity of pLDH assays in detecting and differentiating between various malarial species compared with microscopy. METHODS: Blood samples (n = 124) submitted to our laboratory for routine diagnosis of malaria were included in this study. From each blood sample, two thin films and a quantitative buffy coat (QBC) were made for microscopy. Thin films were stained with Giemsa and acridine orange. The pLDH assay was performed on all the samples according to the manufacturer's instructions. RESULTS: Of the 124 blood samples, 84 were negative by all methods (Giemsa, acridine orange, QBC and pLDH assay). Of the 38 samples positive for Plasmodium falciparum on microscopy, pLDH assay correctly identified 36 at parasite counts as low as < 40 parasites/microl and had a sensitivity and specificity of 94.3% and 97.6%, respectively. Of the 21 samples positive for Plasmodium vivax, pLDH assay correctly identified 19 at parasite counts as low as < 80/microl, and had a sensitivity and specificity of 90.4% and 100%, respectively. However, it failed to identify two Plasmodium vivax infections at parasite counts of 5000/microl and > 200/microl, suggesting that plasmodial gene deletions could be responsible for non-expression of pLDH. CONCLUSIONS: Our data demonstrate that pLDH assay, given its accuracy, rapidity (10-15 minutes), ease of performance and interpretation, can be a useful tool for the detection of malaria in countries where both plasmodial species are co-endemic and where laboratory support is limited.

Animals↗
PubMed2003

Cross-species regulation of Plasmodium parasitemia in semi-immune children from Papua New Guinea.

Malariologists have long been fascinated by the question of whether Plasmodium spp. interact in the human host. The first genetic study of the longitudinal dynamics of multiple Plasmodium spp. and genotypes in humans has been completed in Papua New Guinea, where all four Plasmodium spp. that infect humans are present. The broad implications of the data from this study are covered here and they show that the total parasite density of Plasmodium species oscillates around a threshold and that peaks of infection with each species do not coincide. It is proposed that malaria parasitemia is controlled in a density-dependent manner in these semi-immune children and that a cross-species mechanism of parasite regulation exists. A model of how multiple immune responses could act in concert to explain these within-host dynamics are discussed here in relation to observed epidemiological patterns of mixed-species infections.

Animals↗
PubMed2004

Recombinant expression and enzymatic subsite characterization of plasmepsin 4 from the four Plasmodium species infecting man.

Plasmepsin 4 from Plasmodium falciparum and orthologs from Plasmodium malariae, Plasmodium ovale and Plasmodium vivax have been expressed in recombinant form, and properties of the active site of each enzyme characterized by kinetic analysis. A panel of chromogenic peptide substrates systematically substituted at the P3, P2, P2' and P3' positions was used to estimate enzyme/ligand interactions in the corresponding enzyme subsites based upon kinetic data. The kinetic parameters kcat, Km and kcat/Km were measured to identify optimal substrates for each enzyme and also sequences that were readily cleaved by the plasmepsins but poorly by host aspartic peptidases. Computer generated models were utilized to compare enzyme structures and interpret kinetic results. The orthologous plasmepsins share highly similar subsite specificities. In the S3 and S2 subsites, the plasmepsin 4 orthologs all preferred hydrophobic amino acid residues, Phe or Ile, but rejected charged residues such as Lys or Asp. In S2' and S3' subsites, these plasmepsins tolerated both hydrophobic and hydrophilic residues. Subsite specificities of the plasmepsin 4 family of orthologs are similar to those of human cathepsins D and E, except in S3' where the plasmepsins accept substrates containing Ser significantly better than either of these human aspartic proteases. Peptidomimetic methyleneamino reduced-peptide inhibitors, which have inhibition constants in the picomolar range, were prepared for each plasmepsin 4 ortholog based upon substrate preferences. A peptidomimetic inhibitor designed for plasmepsin 4 from P. falciparum having Ser in P3' had the lowest Ki of the series of inhibitors prepared, but did not significantly improve the selectivity of the inhibitor for plasmepsin 4 versus human cathepsin D.

Animals↗
PubMed2005

A new Apicomplexa-specific protein kinase family: multiple members in Plasmodium falciparum, all with an export signature.

BACKGROUND: Malaria caused by protozoan parasites of the genus Plasmodium spp. is a major health burden in tropical countries. The development of new control tools, including vaccines and drugs, is urgently needed. The availability of genome sequences from several malaria parasite species provides a basis on which to identify new potential intervention targets. Database mining for orthologs to the Plasmodium falciparum trophozoite protein R45, a vaccine candidate, led us identify a new gene family. RESULTS: Orthologs to the P. falciparum trophozoite protein R45 were detected exclusively in protozoan parasites of the phylum Apicomplexa, including several Plasmodium spp., Toxoplasma gondii and Cryptosporidium parvum. All family members are hybrid genes with a conserved C-terminal protein kinase domain of a novel type, recently called FIKK kinase, associated with a non conserved N-terminal region without any known functional signature. While a single copy gene was detected in most species, considerable gene expansion was observed in P. falciparum and its closest phylogenic relative P. reichenowi, with 20 and six copies, respectively, each with a distinct N-terminal domain. Based on full length protein sequence, pairs of orthologs were observed in closely related species, such as P. berghei and P.y. yoelii, P. vivax and P. knowlesi, or P. reichenowi and P. falciparum. All 20 P. falciparum paralogs possess a canonical Plasmodium export element downstream of a signal / anchor sequence required for exportation outside the parasitophorous vacuole. This is consistent with the reported association of the trophozoite protein R45, the only paralog characterised to date, with the infected red blood cell membrane. Interestingly, most genes are located in the subtelomeric region of chromosomes, in association with other multigene families contributing to the remodelling of the infected red blood cell membrane, in particular the ring erythrocyte surface antigen multigene family. CONCLUSION: This Apicomplexan-specific gene family was called R45-FIKK kinase. The family hallmark is a kinase domain with unusual characteristics, raising the possibility of designing drug or vaccine strategies targeting this domain. The characteristics of the P. falciparum family suggest a role in remodelling the infected cell and as such possibly contribute to the particular virulence of this species.

Animals↗
PubMed1988

Circumsporozoite protein gene from Plasmodium brasilianum. Animal reservoirs for human malaria parasites?

We describe here the sequence of the circumsporozoite protein gene of the monkey malaria parasite Plasmodium brasilianum and show that the immunodominant repeat domain is the same as that of the human malaria parasite, Plasmodium malariae. The immunodominant epitope on the surface of sporozoites of a third species of human malaria parasite has, therefore, been identified. This genetic based data and the biological similarities between P. brasilianum and P. malariae support their putative zoonotic/anthroponotic relationship. We also show that an ape malaria parasite, Plasmodium reichenowi, and the human malaria parasite, Plasmodium falciparum, have a similar relationship. The implications of these observations are discussed with respect to vaccine development.

Amino Acid Sequence↗
PubMed1999

Memory phenotype CD8(+) T cells persist in livers of mice protected against malaria by immunization with attenuated Plasmodium berghei sporozoites.

Natural exposure to Plasmodium parasites induces short-lived protective immunity. In contrast, exposure to radiation-attenuated sporozoites (gamma spz) promotes long-lasting protection that is in part mediated by CD8(+) T cells that target exoerythrocytic stage antigens. The mechanisms underlying the maintenance of long-lasting protection are currently unclear. The liver is a repository of Plasmodium antigens and may support the development and / or homing of memory T cells. While activated CD8(+) T cells are presumed to die in the liver, the fate of anti-Plasmodium CD8(+) T cells remains unknown. We propose that inflammatory conditions in the liver caused by Plasmodium parasites may allow some effector CD8(+) T cells to survive and develop into memory cells. To support this hypothesis, in this initial study we demonstrate that liver mononuclear cells from P. berghei gamma spz-immune mice transferred protection to naive recipients and moreover, that CD4(+) and CD8(+) T cells responded to Plasmodium antigens by up-regulating activation / memory markers. While CD4(+) T cells under went a transient activation following immunization with gamma spz, CD8(+) T cells expanded robustly after spz challenge and exhibited stable expression of CD44(hi) and CD45RB(lo) during protracted protection. These results establish a key role for intrahepatic T cells in long-lasting protection against malaria.

Animals↗
PubMed1987

Specific and nonspecific immunodiagnostic properties of recombinant and synthetic Plasmodium falciparum antigens.

Six Plasmodium falciparum/beta-galactosidase fusion proteins produced by a genomic DNA expression library, and two synthetic Plasmodium falciparum antigens were applied to ELISA and tested for their immunodiagnostic properties. Results were compared to reference methods, i.e. fluorescence antibody test with whole cell antigen and ELISA with detergent-soluble crude schizont antigen. Anti-Plasmodium falciparum antibodies could be detected by these molecular antigens to varying extents in human sera. Undesired reactivity to fusion proteins due to the high prevalence of antibodies to beta-galactosidase in human sera and undesired reactivity to one of the synthetic antigens (P12) frequently occurred. The antibodies responsible for the nonspecific reactivity could not be identified. It was concluded that the application of molecular Plasmodium falciparum antigens to ELISA represents a practicable approach to immunodiagnosis of malaria if the construction of epitopes that bind antibodies other than Plasmodium falciparum antibodies can be avoided.

Animals↗
PubMed1991

Cell cycle-dependent biosynthesis of Plasmodium falciparum DNA polymerase-alpha.

The DNA polymerase-alpha of Plasmodium falciparum was characterized according to aphidicolin sensitivity and immunological reactivity with monoclonal anti-sera against human DNA polymerase-alpha. Two major (105 and 72 kDa) and two minor (180 and 130 kDa) catalytic subunits of P. falciparum DNA polymerase-alpha were detected on activity gels. Activity gels did not indicate the presence of a DNA polymerase-beta in P. falciparum. Metabolically labeled polypeptides at 180, 105, 72, and 52 kDa were immunoprecipitated from Plasmodium nuclear extracts with the anti-KB cell DNA polymerase-alpha monoclonal antibody and, by size, correspond to the major subunits of mammalian DNA polymerase-alpha. The monoclonal antibody also neutralized Plasmodium DNA polymerase activity. Plasmodium DNA polymerase was synthesized predominantly at an early schizont stage at which time the parasite began to synthesize its DNA and multiply. No evidence for phosphorylation of the major catalytic subunit was obtained. Plasmodium growth, DNA synthesis, and DNA polymerase activity were inhibited significantly in parallel by aphidicolin. These results suggest that P. falciparum has a typical eukaryotic DNA polymerase-alpha and that regulation of its activity appears to be at the transcriptional level.

Animals↗
PubMed2005

The eukaryotic Pso2p/Snm1p family revisited: in silico analyses of Pso2p A, B and Plasmodium groups.

The eukaryotic family of Pso2/Snm1 exo/endonuclease proteins has important functions in repair of DNA damages induced by chemical interstrand cross-linking agents and ionizing radiation. These exo/endonucleases are also necessary for V(D)J recombination and genomic caretaking. However, despite the growing biochemical data about this family, little is known about the number of orthologous/paralogous Pso2p/Snm1p sequences in eukaryotes and how they are phylogenetically organized. In this work we have characterized new Pso2p/Snm1p sequences from the finished and unfinished eukaryotic genomes and performed an in-depth phylogenetic analysis. The results indicate that four phylogenetically related groups compose the Pso2p/Snm1p family: (i) the Artemis/Artemis-like group, (ii) the Pso2p A group, (iii) the Pso2p B group and (iv) the Pso2p Plasmodium group. Using the available biochemical and genomic information about Pso2p/Snm1p family, we concentrate our research in the study of Pso2p A, B and Plasmodium groups. The phylogenetic results showed that A and B groups can be organized in specific subgroups with different functions in DNA metabolism. Moreover, we subjected selected Pso2p A, B and Plasmodium proteins to hydrophobic cluster analysis (HCA) in order to map and to compare conserved regions within these sequences. Four conserved regions could be detected by HCA, which are distributed along the metallo-beta-lactamase and beta-CASP motifs. Interestingly, both Pso2p A and B proteins are structurally similar, while Pso2p Plasmodium proteins have a unique domain organization. The possible functions of A, B and Plasmodium groups are discussed.

Animals↗
PubMed2005

Unusual properties of Plasmodium falciparum actin: new insights into microfilament dynamics of apicomplexan parasites.

Plasmodium falciparum, the etiologic agent of malaria, is a facultative intracellular parasite of the phylum Apicomplexa. A limited turnover of microfilaments takes place beneath the parasite plasma membrane, but the cytoplasm of apicomplexans is virtually devoid of F-actin. We produced Plasmodium actin in yeast. Purified recombinant Plasmodium actin polymerized inefficiently unless both gelsolin and phalloidin were added. The resulting actin polymers appeared fragmented in the fluorescence microscope. Plasmodium actin bound DNaseI about 200 times weaker than bovine non-muscle actin. Our findings suggest that the unique properties of Plasmodium actin can explain some of the unusual features of apicomplexan parasite microfilaments.

Actins↗
PubMed2000

The effects of subcurative doses of chloroquine on Plasmodium vinckei petteri gametocytes and on their infectivity to mosquitoes.

The effects of subcurative doses of chloroquine on rodent and human Plasmodium transmission to the mosquito have been studied by several authors who showed a short-term (12 h) enhancement of gametocyte infectivity by the drug, restricted to chloroquine-resistant strains, and a long term (4-6 days) enhancement of gametocytogenesis of chloroquine-sensitive strains of Plasmodium chabaudi. We investigated both short- and long-term effects of chloroquine on Plasmodium vinckei petteri, a chloroquine-sensitive rodent Plasmodium strain. Chloroquine treatment reduced the index of gametocytogenesis to 73% (5 mg/kg) and 55% (2.5 mg/kg) of controls, on day 6 post-infection (p.i.). The reduction was statistically significant with 5 mg/kg chloroquine. However, the reduction of gametocyte numbers did not affect the transmission capabilities of the strain. Our experiments showed that doses of 1 mg/kg chloroquine had no effect on the oocyst counts, 12 h post-administration to mice. A statistically non-significant 61% reduction of oocyst numbers was observed in mosquitoes fed on mice treated with 5 mg/kg chloroquine. The effect of 5 mg/kg chloroquine administration on the infectivity of gametocytes to mosquitoes fed 1 h post-treatment was also investigated. An overall 41% reduction of oocyst numbers was observed. This immediate effect was statistically significant in 73% of the mice. These results are consistent with the hypothesis that the short-term enhancing effect of chloroquine on transmission is restricted to the drug-resistant strains of Plasmodium.

Animals↗
PubMed2003

A unique insertion in Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: evolutionary and functional studies.

Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase (G6PD-6PGL) is a bifunctional enzyme with significant sequence similarity in both the 6PGL and G6PD domains to the Plasmodium falciparum enzyme. A recombinant form of the P. berghei enzyme was found to have both G6PD and 6PGL activities, and therefore catalyses the first two steps in the pentose phosphate pathway. Genes encoding very similar proteins are also found in three other malarial parasites, Plasmodium yoelii, Plasmodium chabaudi and Plasmodium knowlesi. All of these predicted enzymes contain unique parasite insertions in corresponding positions in the G6PD domain but the insertions differ in size and sequence. Such insertions are a common feature of malarial proteins but their origin and function is unknown. Excision of the insertion sequence in the P. berghei protein renders the G6PD domain inactive, although the 6PGL activity is unaffected. Replacing the insertion sequence in P. berghei with the insertion sequence from P. falciparum restores some of the G6PD activity and also enhances 6PGL activity. We conclude that although the insertions are evolving rapidly they have an essential role in the activity of the bifunctional enzyme.

Amino Acid Sequence↗
PubMedDate not supplied

Immunisation with recombinant AMA-1 protects mice against infection with Plasmodium chabaudi.

The Plasmodium merozoite surface antigen apical membrane antigen-1 (AMA-1) has previously been shown to provide partial protection to Saimiri and rhesus monkeys immunised with recombinant Plasmodium fragile or parasite-derived Plasmodium knowlesi AMA-1, respectively. In the study reported here we have used the Plasmodium chabaudi/mouse model system to extend our pre-clinical assessment of an AMA-1 vaccine. We describe here the expression of the full-length Plasmodium chabaudi adami AMA-1 and the P. chabaudi adami AMA-1 ectodomain using both baculovirus and Escherichia coli. The ectodomain expressed in E. coli, which contained an N-terminal hexa-his tag, was purified by Ni-chelate chromatography and refolded in vitro in the presence of oxidised and reduced glutathione to generate intramolecular disulphide bonds. In a series of vaccine trials, in both inbred and outbred mice, highly significant protection was obtained by immunising with the refolded AMA-1 ectodomain. Protection was shown to correlate with antibody response and was dependent on intact disulphide bonds. Passive transfer of antibodies raised in rabbits against the refolded AMA-1 ectodomain was also protective. In view of this demonstration that E. coli expression of a soluble P. chabaudi AMA-1 domain can generate a vaccine that is effective in mice, we are pursuing a similar approach to generating a vaccine against P. falciparum for testing in human volunteers.

Animals↗
PubMed1999

IgG reactivities against recombinant Rhoptry-Associated Protein-1 (rRAP-1) are associated with mixed Plasmodium infections and protection against disease in Tanzanian children.

A cross-sectional sero-epidemiological study was performed in Magoda, Tanzania, an area where malaria is holoendemic. Blood samples were collected from children (1-4 years) and tested for IgG antibody reactivity against 2 recombinant protein fragments of Plasmodium falciparum Rhoptry-Associated Protein-1 (rRAP-1). The data were related to the prevalence of malarial disease and single P. falciparum or mixed Plasmodium infections. Fever (> or = 37.5 degrees C) in combination with parasite densities > 5000/microliter were used to distinguish between children with asymptomatic malaria infections and those with acute clinical disease. Furthermore, C-reactive protein (CRP) was applied as a surrogate marker of malaria morbidity. The prevalence of Plasmodium infections was 96.0%. Eleven children were defined as clinical malaria cases, all with single P. falciparum infections. The density of P. falciparum was significantly lower in children with mixed Plasmodium infections compared to those with single P. falciparum infections. Children with asymptomatic P. falciparum infections had higher IgG reactivities to rRAP-1, compared to IgG reactivities of children with malarial disease. Children with mixed Plasmodium infections generally showed elevated IgG reactivity to rRAP-1, when compared to children with single P. falciparum infections. The possible relationship between mixed species infections, clinical outcome of the disease and antibody responses to RAP-1 is discussed.

Age Factors↗
PubMed2002

Substrate specificity of the Plasmodium falciparum glycosylphosphatidylinositol biosynthetic pathway and inhibition by species-specific suicide substrates.

The substrate specificities of the early glycosylphosphatidylinositol biosynthetic enzymes of Plasmodium were determined using substrate analogues of D-GlcN(alpha)1-6-D-myo-inositol-1-HPO(4)-sn-1,2-dipalmitoylglycerol (GlcN-PI). Similarities between the Plasmodium and mammalian (HeLa) enzymes were observed. These are as follows: (i) The presence and orientation of the 2'-acetamido/amino and 3'-OH groups are essential for substrate recognition for the de-N-acetylase, inositol acyltransferase, and first mannosyltransferase enzymes. (ii) The 6'-OH group of the GlcN is dispensable for the de-N-acetylase, inositol acyltransferase, all four of the mannosyltransferases, and the ethanolamine phosphate transferase. (iii) The 4'-OH group of GlcNAc is not required for recognition, but substitution interferes with binding to the de-N-acetylase. The 4'-OH group of GlcN is essential for the inositol acyltransferase and first mannosyltransferase. (iv) The carbonyl group of the natural 2-O-hexadecanyl ester of GlcN-(acyl)PI is essential for substrate recognition by the first mannosyltransferase. However, several differences were also discovered: (i) Plasmodium-specific inhibition of the inositol acyltransferase was detected with GlcN-[L]-PI, while GlcN-(2-O-alkyl)PI weakly inhibited the first mannosyltransferase in a competitive manner. (ii) The Plasmodium de-N-acetylase can act on analogues containing N-benzoyl, GalNAc, or betaGlcNAc whereas the human enzyme cannot. Using the parasite specificity of the later two analogues with the known nonspecific de-N-acetylase suicide inhibitor [Smith, T. K., et al. (2001) EMBO J. 20, 3322-3332], GalNCONH(2)-PI and GlcNCONH(2)-beta-PI were designed and found to be potent (IC(50) approximately 0.2 microM), Plasmodium-specific suicide substrate inhibitors. These inhibitors could be potential lead compounds for the development of antimalaria drugs.

Acyltransferases↗
PubMed2005

Structure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH.

Malaria caused by Plasmodium vivax is a major cause of global morbidity and, in rare cases, mortality. Lactate dehydrogenase is an essential Plasmodium protein and, therefore, a potential antimalarial drug target. Ideally, drugs directed against this target would be effective against both major species of Plasmodium, P. falciparum and P. vivax. In this study, the crystal structure of the lactate dehydrogenase protein from P. vivax has been solved and is compared to the equivalent structure from the P. falciparum enzyme. The active sites and cofactor binding pockets of both enzymes are found to be highly similar and differentiate these enzymes from their human counterparts. These structures suggest effective inhibition of both enzymes should be readily achievable with a common inhibitor. The crystal structures of both enzymes have also been solved in complex with the synthetic cofactor APADH. The unusual cofactor binding site in these Plasmodium enzymes is found to readily accommodate both NADH and APADH, explaining why the Plasmodium enzymes retain enzymatic activity in the presence of this synthetic cofactor.

Animals↗
PubMed1981

Immunity to Plasmodium chabaudi adami in the B-cell-deficient mouse.

Immunity to malaria has a multicomponent basis which requires the participation of both T- and B-lymphocyte systems. Previous studies have suggested that the T-lymphocyte system has an essential role in 're-infection immunity' to malaria, but that B cells and/or their products are necessary for the host to survive acute infection and to clear the blood of parasites during chronic malaria. Thus, B-cell-deficient mice and chickens died of fulminant malaria when infected with Plasmodium yoelii and Plasmodium gallinaceum, respectively, but when their acute infections were controlled with subcurative chemotherapy, B-cell-deficient host developed chronic low-grade infections and resisted challenge with homologous parasites. In contrast, athymic nude mice failed to control their endogenous P. yoelii infection after the termination of drug therapy unless they had been thymus grafted before initiation of acute infection. We now report that Plasmodium chabaudi adami (556KA) infection in B-cell-deficient mice results in an activation of a T-cell-dependent immune mechanism which terminates acute malaria in a similar way to that seen in immunologically intact mice. Furthermore, these immunized B-cell-deficient mice were resistant to homologous challenge infection as well as infections initiated with Plasmodium vinckei, but not with P. yoelii and Plasmodium berghei.

Animals↗
PubMed2003

The energetic budget of Anopheles stephensi infected with Plasmodium chabaudi: is energy depletion a mechanism for virulence?

Evidence continues to accumulate showing that the malaria parasites (Plasmodium spp.) reduce the survival and fecundity of their mosquito vectors (Anopheles spp.). Our ability to identify the possible epidemiological and evolutionary consequences of these parasite-induced fitness reductions has been hampered by a poor understanding of the physiological basis of these shifts. Here, we explore whether the reductions in fecundity and longevity are the result of a parasite-mediated depletion or reallocation of the energetic resources of the mosquito. Mosquitoes infected with Plasmodium chabaudi were expected to have less energetic resources than uninfected mosquitoes, and energy levels were predicted to be lowest in mosquitoes infected with the most virulent parasite genotypes. Not only was there no evidence of a parasite-mediated reduction in the overall energetic budget of mosquitoes, but Plasmodium was actually associated with increased levels of glucose, a key insect nutritional and energetic resource. The data strongly suggest the existence of an increase in sugar feeding in mosquitoes infected with Plasmodium. We suggest different adaptive explanations for an enhanced sugar uptake in infected mosquitoes and call for more studies to investigate the physiological role of glucose in the Plasmodium-mosquito interaction.

Adaptation, Physiological↗