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Academic literature on the topic 'Plasmodial Proteins'

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Published: 6 September 2023

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Journal articles on the topic "Plasmodial Proteins"

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Musyoka, Thommas, and Özlem Tastan Bishop. "South African Abietane Diterpenoids and Their Analogs as Potential Antimalarials: Novel Insights from Hybrid Computational Approaches." Molecules 24, no. 22 (November 7, 2019): 4036. http://dx.doi.org/10.3390/molecules24224036.

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The hemoglobin degradation process in Plasmodium parasites is vital for nutrient acquisition required for their growth and proliferation. In P. falciparum, falcipains (FP-2 and FP-3) are the major hemoglobinases, and remain attractive antimalarial drug targets. Other Plasmodium species also possess highly homologous proteins to FP-2 and FP-3. Although several inhibitors have been designed against these proteins, none has been commercialized due to associated toxicity on human cathepsins (Cat-K, Cat-L and Cat-S). Despite the two enzyme groups sharing a common structural fold and catalytic mechanism, distinct active site variations have been identified, and can be exploited for drug development. Here, we utilize in silico approaches to screen 628 compounds from the South African natural sources to identify potential hits that can selectively inhibit the plasmodial proteases. Using docking studies, seven abietane diterpenoids, binding strongly to the plasmodial proteases, and three additional analogs from PubChem were identified. Important residues involved in ligand stabilization were identified for all potential hits through binding pose analysis and their energetic contribution determined by binding free energy calculations. The identified compounds present important scaffolds that could be further developed as plasmodial protease inhibitors. Previous laboratory assays showed the effect of the seven diterpenoids as antimalarials. Here, for the first time, we demonstrate that their possible mechanism of action could be by interacting with falcipains and their plasmodial homologs. Dynamic residue network (DRN) analysis on the plasmodial proteases identified functionally important residues, including a region with high betweenness centrality, which had previously been proposed as a potential allosteric site in FP-2.
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Gayathri, P., Hemalatha Balaram, and MRN Murthy. "Structural biology of plasmodial proteins." Current Opinion in Structural Biology 17, no. 6 (December 2007): 744–54. http://dx.doi.org/10.1016/j.sbi.2007.08.001.

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Shonhai, Addmore. "Plasmodial heat shock proteins: targets for chemotherapy." FEMS Immunology & Medical Microbiology 58, no. 1 (February 2010): 61–74. http://dx.doi.org/10.1111/j.1574-695x.2009.00639.x.

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Adisa, Akinola, Frank R. Albano, John Reeder, Michael Foley, and Leann Tilley. "Evidence for a role for a Plasmodium falciparum homologue of Sec31p in the export of proteins to the surface of malaria parasite-infected erythrocytes." Journal of Cell Science 114, no. 18 (September 15, 2001): 3377–86. http://dx.doi.org/10.1242/jcs.114.18.3377.

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The malaria parasite, Plasmodium falciparum, spends part of its life cycle inside the enucleated erythrocytes of its human host. The parasite modifies the cytoplasm and plasma membrane of its host cell by exporting proteins beyond the confines of its own plasma membrane. We have previously provided evidence that a plasmodial homologue of the COPII protein, Sar1p, is involved in the trafficking of proteins across the erythrocyte cytoplasm. We have now characterised an additional plasmodial COPII protein homologue, namely Sec31p. Recombinant proteins corresponding to the WD-40 and the intervening domains of the PfSec31p sequence were used to raise antibodies. The affinity-purified antisera recognised a protein with an apparent relative molecular mass of 1.6×105 on western blots of malaria parasite-infected erythrocytes but not on blots of uninfected erythrocytes. PfSec31p was shown to be largely insoluble in nonionic detergent, suggesting cytoskeletal attachment. Confocal immunofluorescence microscopy of malaria parasite-infected erythrocytes was used to show that PfSec31p is partly located within the parasite and partly exported to structures outside the parasite in the erythrocyte cytoplasm. We have also shown that PfSec31p and PfSar1p occupy overlapping locations. Furthermore, the location of PfSec31p overlaps that of the cytoadherence-mediating protein PfEMP1. These data support the suggestion that the malaria parasite establishes a vesicle-mediated trafficking pathway outside the boundaries of its own plasma membrane – a novel paradigm in eukaryotic biology.
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Pizzi, Elisabetta, and Clara Frontali. "Low-Complexity Regions in Plasmodium falciparum Proteins." Genome Research 11, no. 2 (January 18, 2001): 218–29. http://dx.doi.org/10.1101/gr.152201.

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Full-sequence data available for Plasmodium falciparumchromosomes 2 and 3 are exploited to perform a statistical analysis of the long tracts of biased amino acid composition that characterize the vast majority of P. falciparum proteins and to make a comparison with similarly defined tracts from other simple eukaryotes. When the relatively minor subset of prevalently hydrophobic segments is discarded from the set of low-complexity segments identified by current segmentation methods in P. falciparum proteins, a good correspondence is found between prevalently hydrophilic low-complexity segments and the species-specific, rapidly diverging insertions detected by multiple-alignment procedures when sequences of bona fide homologs are available. Amino acid preferences are fairly uniform in the set of hydrophilic low-complexity segments identified in the twoP. falciparum chromosomes sequenced, as well as in sequenced genes from Plasmodium berghei, but differ from those observed in Saccharomyces cerevisiae and Dictyostelium discoideum. In the two plasmodial species, amino acid frequencies do not correlate with properties such as hydrophilicity, small volume, or flexibility, which might be expected to characterize residues involved in nonglobular domains but do correlate with A-richness in codons. An effect of phenotypic selection versus neutral drift, however, is suggested by the predominance of asparagine over lysine.
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Wunderlich, Gerhard, Fabiana P. Alves, Uta Gölnitz, Mauro S. Tada, Erney F. P. de Camargo, and Luiz H. Pereira-da-Silva. "Rapid turnover of Plasmodium falciparum var gene transcripts and genotypes during natural non-symptomatic infections." Revista do Instituto de Medicina Tropical de São Paulo 47, no. 4 (August 2005): 195–201. http://dx.doi.org/10.1590/s0036-46652005000400004.

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The var genes of Plasmodium falciparum code for the antigenically variant erythrocyte membrane proteins 1 (PfEMP1), a major factor for cytoadherence and immune escape of the parasite. Herein, we analyzed the var gene transcript turnover in two ongoing, non-symptomatic infections at sequential time points during two weeks. The number of different circulating genomes was estimated by microsatellite analyses. In both infections, we observed a rapid turnover of plasmodial genotypes and var transcripts. The rapidly changing repertoire of var transcripts could have been caused either by swift elimination of circulating var-transcribing parasites stemming from different or identical genetic backgrounds, or by accelerated switching of var gene transcription itself.
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Birkholtz, Lyn-Marie, Gregory Blatch, Theresa L. Coetzer, Heinrich C. Hoppe, Esmaré Human, Elizabeth J. Morris, Zoleka Ngcete, et al. "Heterologous expression of plasmodial proteins for structural studies and functional annotation." Malaria Journal 7, no. 1 (2008): 197. http://dx.doi.org/10.1186/1475-2875-7-197.

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PESCE, E. R., and G. L. BLATCH. "Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives." Parasitology 141, no. 9 (March 25, 2014): 1167–76. http://dx.doi.org/10.1017/s003118201300228x.

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SUMMARYPlasmodium falciparumdisplays a large and remarkable variety of heat shock protein 40 family members (PfHsp40s). The majority of the PfHsp40s are poorly characterized, and although the functions of some of them have been suggested, their exact mechanism of action is still elusive and their interacting partners and client proteins are unknown. TheP. falciparumheat shock protein 70 family members (PfHsp70s) have been more extensively characterized than the PfHsp40s, with certain members shown to function as molecular chaperones. However, little is known about the PfHsp70-PfHsp40 chaperone partnerships. There is mounting evidence that these chaperones are important not only in protein homoeostasis and cytoprotection, but also in protein trafficking across the parasitophorous vacuole (PV) and into the infected erythrocyte. We propose that certain members of these chaperone families work together to maintain exported proteins in an unfolded state until they reach their final destination. In this review, we critically evaluate what is known and not known about PfHsp40s and PfHsp70s.
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Lindner, Jasmin, Kamila Anna Meissner, Isolmar Schettert, and Carsten Wrenger. "Trafficked Proteins—Druggable inPlasmodium falciparum?" International Journal of Cell Biology 2013 (2013): 1–13. http://dx.doi.org/10.1155/2013/435981.

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Malaria is an infectious disease that results in serious health problems in the countries in which it is endemic. Annually this parasitic disease leads to more than half a million deaths; most of these are children in Africa. An effective vaccine is not available, and the treatment of the disease is solely dependent on chemotherapy. However, drug resistance is spreading, and the identification of new drug targets as well as the development of new antimalarials is urgently required. Attention has been drawn to a variety of essential plasmodial proteins, which are targeted to intra- or extracellular destinations, such as the digestive vacuole, the apicoplast, or into the host cell. Interfering with the action or the transport of these proteins will impede proliferation of the parasite. In this mini review, we will shed light on the present discovery of chemotherapeutics and potential drug targets involved in protein trafficking processes in the malaria parasite.
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Chen, Xinlu, Tobias G. Köllner, Wangdan Xiong, Guo Wei, and Feng Chen. "Emission and biosynthesis of volatile terpenoids from the plasmodial slime mold Physarum polycephalum." Beilstein Journal of Organic Chemistry 15 (November 28, 2019): 2872–80. http://dx.doi.org/10.3762/bjoc.15.281.

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Terpene synthases (TPSs) are pivotal enzymes for the production of diverse terpenes, including monoterpenes, sesquiterpenes, and diterpenes. In our recent studies, dictyostelid social amoebae, also known as cellular slime molds, were found to contain TPS genes for making volatile terpenes. For comparison, here we investigated Physarum polycephalum, a plasmodial slime mold also known as acellular amoeba. Plasmodia of P. polycephalum grown on agar plates were found to release a mixture of volatile terpenoids consisting of four major sesquiterpenes (α-muurolene, (E)-β-caryophyllene, two unidentified sesquiterpenoids) and the monoterpene linalool. There were no qualitative differences in terpenoid composition at two stages of young plasmodia. To understand terpene biosynthesis, we analyzed the transcriptome and genome sequences of P. polycephalum and identified four TPS genes designated PpolyTPS1–PpolyTPS4. They share 28–73% of sequence identities. Full-length cDNAs for the four TPS genes were cloned and expressed in Escherichia coli to produce recombinant proteins, which were tested for sesquiterpene synthase and monoterpene synthase activities. While neither PpolyTPS2 nor PpolyTPS3 was active, PpolyTPS1 and PpolyTPS4 were able to produce sesquiterpenes and monoterpenes from the respective substrates farnesyl diphosphate and geranyl diphosphate. By comparing the volatile profile of P. polycephalum plasmodia and the in vitro products of PpolyTPS1 and PpolyTPS4, it was concluded that most sesquiterpenoids emitted from P. polycephalum were attributed to PpolyTPS4. Phylogenetic analysis placed the four PpolyTPSs genes into two groups: PpolyTPS1 and PpolyTPS4 being one group that was clustered with the TPSs from the dictyostelid social amoeba and PpolyTPS2 and PpolyTPS3 being the other group that showed closer relatedness to bacterial TPSs. The biological role of the volatile terpenoids produced by the plasmodia of P. polycephalum is discussed.
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Dissertations / Theses on the topic "Plasmodial Proteins"

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Yap, Jessica. "Identification of Plasmodium falciparum protein kinase substrates and interacting proteins." Honors in the Major Thesis, University of Central Florida, 2012. http://digital.library.ucf.edu/cdm/ref/collection/ETH/id/644.

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Characterization of PfPKA and PfPK5 substrates, as well as the proteins they interact with, will help us to develop innovative therapies targeting binding sites.; Malaria is a devastating disease that results in almost one million deaths annually. Most of the victims are children under the age of five in Sub-Saharan Africa. Malaria parasite strains throughout developing countries are continually building resistance to available drugs. Current therapies such as mefloquine, chloroquine, as well as artemisinin are becoming less effective, and this underscores the urgency for therapeutics directed against novel drug targets. In order to identify new drug targets, the molecular biology of the malaria parasite Plasmodium needs to be elucidated. Plasmodium exhibits a unique cell cycle in which it undergoes multiple rounds of DNA synthesis and mitosis without cytokinesis. Thus, cell cycle regulatory proteins are likely to be promising pathogen-specific drug targets. It is expected that fluctuating activity of key proteins, such as protein kinases, play an essential role in regulating the noncanonical life cycle of Plasmodium. Consequently, malarial kinases are a prime target for therapy. One way to better understand the role of malarial kinases in Plasmodium cell cycle regulation is to identify putative protein kinase substrates and interacting proteins. Two malarial kinases that have been implicated in regulating malaria parasite cell cycle stages were investigated in this study: P. falciparum CDK-like Protein Kinase 5 (PfPK5) and cAMP-Dependent Protein Kinase A (PfPKA). A transgenic P. falciparum line was created for the expression of epitope-tagged PfPK5 for pull-down analysis. Phospho-substrate antibodies were used to identify physiological substrates of both PfPK5 and PfPKA. Immunoblotting with these antibodies identified several potential substrates. Identities of the PfPKA physiological substrates were determined from the global P. falciparum phosphoproteome dataset that has recently been generated in our laboratory.
B.S.
Bachelors
Burnett School of Biomedical Sciences
Molecular and Microbiology
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Shonhai, Addmore. "Molecular characterisation of the chaperone properties of Plasmodium falciparum heat shock protein 70." Thesis, Rhodes University, 2007. http://eprints.ru.ac.za/886/.

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Matambo, Tonderayi Sylvester. "Biochemical characterization of plasmodium falciparum heat shock protein 70." Thesis, Rhodes University, 2004. http://eprints.ru.ac.za/73/1/Matambo-MSc.pdf.

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Plamodium falciparum heat shock protein (PfHsp70) is believed to be involved in the cytoprotection of the malaria parasite through its action as a molecular chaperone. Bioinformatic analysis reveal that PfHsp70 consists of the three canonical Hsp70 domains; an ATPase domain of 45 kDa, Substrate binding domain of 15 kDa and a C-terminal domain of 10 kDa. At the C-terminus there is a GGMP repeat motif that is commonly found in Hsp70s of parasitic origins. Plasmodium falciparum genome is 80% A-T rich, making it difficult to recombinantly express its proteins in Escherhia coli (E. coli) as a result of rare codon usage. In this study we carried out experiments to improve expression in E. coli by inserting the PfHsp70 coding region into the pQE30 expression vector. However multiple bands were detected by Western analysis, probably due to the presence of rare codons. The RIG plasmid, which encodes tRNAs for rare codons in particular Arg (AGA/AGG), Ile (AUA) and Gly (GGA) was engineered into the E. coli strain resulting in production of full length PfHsp70. Purification was achieved through Ni^(2+) Chelating sepharose under denaturing conditions. PfHsp70 was found to have a very low basal ATPase activity of 0.262 ± 0.05 nmoles/min/mg of protein. In the presence of reduced and carboxymethylated lactalbumin (RCMLA) a 11-fold increase in ATPase activity was noted whereas in the presence of both RCMLA and Trypanosoma cruzi DnaJ (Tcj2) a 16-fold was achieved. For ATP hydrolysis kcat value of 0.003 min^(-1) was obtained whereas for ADP release a greater k_cat_ value of 0.8 min^(-1) was obtained. These results indicated that rate of ATP hydrolysis maybe the rate-determining step in the ATPase cycle of PfHsp70.
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Stubberfield, Lisa Marie. "Interactions of Plasmodium falciparum proteins at the membrane skeleton of infected erythrocytes." Monash University, Dept. of Microbiology, 2003. http://arrow.monash.edu.au/hdl/1959.1/9433.

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Holton, S. J. "Structural and functional studies of Plasmodium falciparum protein kinase 5 and Cks proteins." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270634.

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McNamara, Caryn. "Characterisation of Human Hsj1a : an HSP40 molecular chaperone similar to Malarial Pfj4." Thesis, Rhodes University, 2007. http://hdl.handle.net/10962/d1007603.

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Protein folding, translocation, oligomeric rearrangement and degradation are vital functions to obtain correctly folded proteins in any cell. The constitutive or stress-induced members of each of the heat shock protein (Hsp) families, namely Hsp70 and Hsp40, make up the Hsp70/Hsp40 chaperone system. The Hsp40 J-domain is important for the Hsp70-Hsp40 interaction and hence function. The type-II Hsp40 proteins, Homo sapiens DnaJ 1a (Hsj1a) and Plasmodium falciparum DnaJ 4 (Pfj4), are structurally similar suggesting possible similar roles during malarial infection. This thesis has focussed on identifying whether Hsj1a and Pfj4 are functionally similar in their interaction with potential partner Hsp70 chaperones. Analysis in silico also showed Pfj4 to have a potential chaperone domain, a region resembling a ubiquitin-interacting motif (UIM) corresponding to UIM1 of HsjIa, and another highly conserved region was noted between residues 232-241. The highly conserved regions within the Hsp40 J-domains, and those amino acids therein, are suggested to be responsible for mediating this Hsp70-Hsp40 partner interaction. The thermosensitive dnaJ cbpA Escherichia coli OD259 mutant strain producing type-I Agrobacterium tumefaciens DnaJ (AgtDnaJ) was used as a model heterologous expression system in this study. AgtDnaJ was able to replace the lack of two E coli Hsp40s in vivo, DnaJ and CbpA, whereas AgtDnaJ(H33Q) was unable to. AgtDnaJ-based chimeras containing the swapped J-domains of similar type-II Hsp40 proteins, namely Hsj1Agt and Pfj4Agt, were also able to replace these in E. coli OD259. Conserved J-domain amino acids were identified and were substituted in these chimeras. Of these mutant proteins, Hsj IAgt(L8A), Hsj1Agt(R24A), Hsj1Agt(H31Q), Pfj4Agt(L 11A) and Pfj4Agt(H34Q) were not able to replace the E. coli Hsp40s, whilst Pfj4Agt(Y8A) and Pfj4Agt(R27A) were only able to partially replace them. This shows the leucine of helix I and the histidine of the loop region are key in the in vivo function of both proteins and that the arginine of helix II is key for Hsj1a. The histidine-tagged Hsj1a protein was also successfully purified from the heterologous system. The in vitro stimulated ATPase activity of human Hsp70 by Hsj1a was found to be approximately 14 nmol Pí[subscript]/min/mg, and yet not stimulated by Pfj4, suggesting a possible species-specific interaction is occurring.
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Botha, Melissa. "Characterisation of the plasmodium falciparum Hsp40 chaperones and their partnerships with Hsp70." Thesis, Rhodes University, 2009. http://hdl.handle.net/10962/d1003997.

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Central to this research, 40 kDa Heat shock proteins (Hsp40s) are known to partner (or cochaperone) 70 kDa Heat shock proteins (Hsp70s), facilitating the selection and transfer of protein substrate to Hsp70 and the stimulation of the protein folding ability of Hsp70. Members of the diverse Hsp70-Hsp40 protein complement of Plasmodium falciparum have been implicated in the cytoprotection of this malaria parasite, and are thought to facilitate the protein folding, assembly and translocation tasks required by the parasite to commandeer the infected human erythrocyte subsequent to invasion. In particular, the parasite has evolved an expanded and specialised 43- member suite of Hsp40 proteins, 19 of which bear an identifiable export motif for secretion into the infected erythrocyte cytoplasm where they potentially interact with human Hsp70. Although type I Hsp40 proteins are representative of typical regulators of Hsp70 activity, only two of these proteins are apparent in the parasite’s Hsp40 complement. These include a characteristic type I Hsp40 termed PfHsp40, and a larger, atypical type I Hsp40 termed Pfj1. Both Hsp40 proteins are predicted to be parasite-resident and are most likely to facilitate the co-chaperone regulation of the highly abundant and stress-inducible Hsp70 homolog, PfHsp70-I. In this work, the co-chaperone functionality of PfHsp40 and Pfj1 was elucidated using in vivo and in vitro assays. Purified recombinant PfHsp40 was shown to stimulate the ATPase activity of PfHsp70-I in in vitro single turnover and steady state ATPase assays, and co-operate with PfHsp70-I in in vitro aggregation suppression assays. In these in vitro assays, heterologous partnerships could be demonstrated between PfHsp70-I and the human Hsp40, Hsj1a, and human Hsp70 and PfHsp40, suggesting a common mode of Hsp70-Hsp40 interaction in the parasite and host organism. The functionality of the signature Hsp40 domain, the Jdomain, of Pfj1 was demonstrated by its ability to replace the equivalent domain of the A. tumefaciens Hsp40, Agt DnaJ, in interactions with the prokaryotic Hsp70, DnaK, in the thermosensitive dnaJ cbpA E. coli OD259 deletion strain. An H33Q mutation introduced into the invariant and crucial HPD tripeptide motif abrogated the functionality of the J-domain in the in vivo complementation system. These findings provide the first evidence for the conservation of the prototypical mode of J-domain based interaction of Hsp40 with Hsp70 in P. falciparum. Immunofluorescence staining revealed the localisation of PfHsp40 to the parasite cytoplasm, and Pfj1 to the parasite cytoplasm and nucleus in cultured intraerythrocytic stage P. falciparum parasites. PfHsp70-I was also shown to localise to the parasite cytoplasm and nucleus in these stages, consistent with the literature. Overall we propose that PfHsp40 and Pfj1 co-localise with and regulate the chaperone activity of PfHsp70-I in P. falciparum. This is the first study to identify and provide evidence for a functional Hsp70-Hsp40 partnership in P. falciparum, and provides a platform for future studies to elucidate the importance of these chaperone partnerships in the establishment and survival of the parasite in the intraerythrocytic-stages of development.
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Njunge, James Mwangi. "Characterization of the Hsp40 partner proteins of Plasmodium falciparum Hsp70." Thesis, Rhodes University, 2014. http://hdl.handle.net/10962/d1013186.

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Human malaria is an economically important disease caused by single-celled parasites of the Plasmodium genus whose biology displays great evolutionary adaptation to both its mammalian host and transmitting vectors. This thesis details the 70 kDa heat shock protein (Hsp70) and J protein chaperone complements in malaria parasites affecting humans, primates and rodents. Heat shock proteins comprise a family of evolutionary conserved and structurally related proteins that play a crucial role in maintaining the structural integrity of proteins during normal and stress conditions. They are considered future therapeutic targets in various cellular systems including Plasmodium falciparum. J proteins (Hsp40) canonically partner with Hsp70s during protein synthesis and folding, trafficking or targeting of proteins for degradation. However, in P. falciparum, these classes of proteins have also been implicated in aiding the active transport of parasite proteins to the erythrocyte cytosol following erythrocyte entry by the parasite. This host-parasite “cross-talk” results in tremendous modifications of the infected erythrocyte, imparting properties that allow it to adhere to the endothelium, preventing splenic clearance. The genome of P. falciparum encodes six Hsp70 homologues and a large number of J proteins that localize to the various intracellular compartments or are exported to the infected erythrocyte cytosol. Understanding the Hsp70-J protein interactions and/or partnerships is an essential step for drug target validation and illumination of parasite biology. A review of these chaperone complements across the Plasmodium species shows that P. falciparum possesses an expanded Hsp70-J protein complement compared to the rodent and primate infecting species. It further highlights how unique the P. falciparum chaperone complement is compared to the other Plasmodium species included in the analysis. In silico analysis showed that the genome of P. falciparum encodes approximately 49 J proteins, 19 of which contain a PEXEL motif that has been implicated in routing proteins to the infected erythrocyte. Most of these PEXEL containing J proteins are unique with no homologues in the human system and are considered as attractive drug targets. Very few of the predicted J proteins in P. falciparum have been experimentally characterized. To this end, cell biological and biochemical approaches were employed to characterize PFB0595w and PFD0462w (Pfj1) J proteins. The uniqueness of Pfj1 and the controversy in literature regarding its localization formed the basis for the experimental work. This is the first study showing that Pfj1 localizes to the mitochondrion in the intraerythrocytic stage of development of P. falciparum and has further proposed PfHsp70-3 as a potential Hsp70 partner. Indeed, attempts to heterologously express and purify Pfj1 for its characterization are described. It is also the first study that details the successful expression and purification of PfHsp70-3. Further, research findings have described for the first time the expression and localization of PFB0595w in the intraerythrocytic stages of P. falciparum development. Based on the cytosolic localization of both PFB0595w and PfHsp70-1, a chaperone – cochaperone partnership was proposed that formed the basis for the in vitro experiments. PFB0595w was shown for the first time to stimulate the ATPase activity of PfHsp70-1 pointing to a functional interaction. Preliminary surface plasmon spectroscopy analysis has revealed a potential interaction between PFB0595w and PfHsp70-1 but highlights the need for further related experiments to support the findings. Gel filtration analysis showed that PFB0595w exists as a dimer thereby confirming in silico predictions. Based on these observations, we conclude that PFB0595w may regulate the chaperone activity of PfHsp70-1 in the cytosol while Pfj1 may play a co-chaperoning role for PfHsp70-3 in the mitochondrion. Overall, this data is expected to increase the knowledge of the Hsp70-J protein partnerships in the erythrocytic stage of P. falciparum development, thereby enhancing the understanding of parasite biology.
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Clitheroe, Crystal-Leigh. "In-silico analysis of Plasmodium falciparum Hop protein and its interactions with Hsp70 and Hsp90." Thesis, Rhodes University, 2013. http://hdl.handle.net/10962/d1003819.

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A lessor understood co-chaperone, the Hsp70/Hsp90 organising protein (Hop), has been found to play an important role in modulating the activity and co-interaction of two essential chaperones; Hsp90 and Hsp70. The best understood aspects of Hop so far indicate that residues in the concave surfaces of the three tetratricopeptide repeat (TPR) domains in the protein bind selectively to the C-terminal motifs of Hsp70 and Hsp90. Recent research suggests that P. falciparum Hop (PfHop), PfHsp90 and PfHsp70 do interact and form complex in the P. falciparum trophozooite and are overexpressed in this infective stage. However, there has been almost no computational research on malarial Hop protein in complex with other malarial Hsps.The current work has focussed on several aspects of the in-silico characterisation of PfHop, including an in-depth multiple sequence alignment and phylogenetic analysis of the protein; which showed that Hop is very well conserved across a wide range of available phyla (four Kingdoms, 60 species). Homology modelling was employed to predict several protein structures for these interactions in P. falciparum, as well as predict structures of the relevant TPR domains of Human Hop (HsHop) in complex with its own Hsp90 and Hsp70 C-terminal peptide partners for comparison. Protein complex interaction analyses indicate that concave TPR sites bound to the C-terminal motifs of partner proteins are very similar in both species, due to the excellent conservation of the TPR domain’s “double carboxylate binding clamp”. Motif analysis was combined with phylogenetic trees and structure mapping in novel ways to attain more information on the evolutionary conservation of important structural and functional sites on Hop. Alternative sites of interaction between Hop TPR2 and Hsp90’s M and C domains are distinctly less well conserved between the two species, but still important to complex formation, making this a likely interaction site for selective drug targeting. Binding and interaction energies for all modelled complexes have been calculated; indicating that all HsHop TPR domains have higher affinities for their respective C-terminal partners than do their P. falciparum counterparts. An alternate motif corresponding to the C-terminal motif of PfHsp70-x (exported to the infected erythrocyte cytosol) in complex with both human and malarial TPR1 and TPR2B domains was analysed, and these studies suggest that the human TPR domains have a higher affinity for this motif than do the respective PfHop TPR domains. This may indicate potential for a cross species protein interaction to take place, as PfHop is not transported to the human erythrocyte cytosol.
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Maphumulo, Philile Nompumelelo. "Characterisation of a plasmodium falciparum type II Hsp40 chaperone exported to the cytosol of infected erythrocytes." Thesis, Rhodes University, 2013. http://hdl.handle.net/10962/d1015681.

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Heat Shock 40 kDa proteins (Hsp40s) partner with heat shock 70 kDa proteins (Hsp70s) in facilitating, among other chaperone activities; correct protein transport, productive protein folding and assembly within the cells; under both normal and stressful conditions. Hsp40 proteins regulate the ATPase activity of Hsp70 through interaction with the J-domain. Plasmodium falciparum Hsp70s (PfHsp70s) do not contain a Plasmodium export element (PEXEL) sequence although PfHsp70-1 and PfHsp70-3 have been located outside of the parasitophorous vacuole. Studies reveal that a type I P. falciparum (PfHsp40) chaperone (PF14_0359) stimulates the rate of ATP hydrolysis of the cytosolic PfHsp70 (PfHsp70-1) and that of human Hsp70A1A. PFE0055c is a PEXEL-bearing type II Hsp40 that is exported into the cytosol of P. falciparum-infected erythrocytes; where it potentially interacts with human Hsp70. Studies reveal that PFE0055c associates with structures found in the erythrocyte cytosol termed “J-dots” which are believed to be involved in trafficking parasite-encoded proteins through the erythrocyte cytosol. If P. falciparum exports PFE0055c into the host cytosol, it may be proposed that it interacts with human Hsp70, making it a possible drug target. The effect of PFE0055c on the ATPase activity of human Hsp70A1A has not been previously characterised. Central to this study was bioinformatic analysis and biochemical characterisation PFE0055c using an in vitro (ATPase assay) approach. Structural domains that classify PFE0055c as a type II Hsp40 were identified with similarity to two other exported type II PfHsp40s. Plasmids encoding the hexahistidine-tagged versions of PFE0055c and human Hsp70A1A were used for the expression and purification of these proteins from Escherichia coli. Purification was achieved using nickel affinity chromatography. The urea-denaturing method was used to obtain the purified PFE0055c whilst human Hsp70A1A was purified using the native method. PFE0055c could stimulate the ATPase activity of alfalfa Hsp70, although such was not the case for human Hsp70A1A in vitro.
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Books on the topic "Plasmodial Proteins"

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Verrall, B. Expresssion of the TATA box binding protein of plasmodium falciparum in heterologous systems. Manchester: UMIST, 1997.

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Malaria resistance or susceptibility in red cells disorders. Hauppauge, NY: Nova Science, 2009.

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Book chapters on the topic "Plasmodial Proteins"

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Liu, Kaiyin, and Walid A. Houry. "Chaperones and Proteases of Plasmodium falciparum." In Heat Shock Proteins of Malaria, 161–87. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7438-4_9.

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Shahinas, Dea, and Dylan R. Pillai. "Role of Hsp90 in Plasmodium falciparum Malaria." In Heat Shock Proteins of Malaria, 87–97. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7438-4_5.

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Mbengue, Alassane, Laurence Berry, and Catherine Braun-Breton. "Establishment of Plasmodium falciparum Extracellular Compartments in its Host Erythrocyte." In Heat Shock Proteins of Malaria, 133–59. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7438-4_8.

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Shonhai, Addmore. "The Role of Hsp70s in the Development and Pathogenicity of Plasmodium Species." In Heat Shock Proteins of Malaria, 47–69. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7438-4_3.

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Kilejian, A., Y. D. Sharma, and Y. F. Yang. "The Knob Protein Gene of Plasmodium Falciparum." In Host-Parasite Cellular and Molecular Interactions in Protozoal Infections, 307–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72840-2_35.

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Doerig, Christian. "Protein Kinases Regulating Plasmodium Proliferation and Development." In Molecular Approaches to Malaria, 290–310. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555817558.ch15.

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Przyborski, Jude. "The Importance of Molecular Chaperones in Survival and Pathogenesis of the Malaria Parasite Plasmodium falciparum." In Heat Shock Proteins of Malaria, 1–3. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7438-4_1.

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Hatano, Sadashi. "Actin, Myosin, and the Associated-Proteins from the Physarum Plasmodium." In The Molecular Biology of Physarum polycephalum, 165–74. Boston, MA: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4613-2203-0_9.

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Bozdech, Zbynek, and Erwin Schurr. "Protein Transport in the Host Cell Cytoplasm and ATP-Binding Cassette Proteins in Plasmodium Falciparum-Infected Erythrocytes." In Novartis Foundation Symposium 226 - Transport and Trafficking in the Malaria-Infected Erythrocyte, 231–51. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515730.ch16.

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Howard, Russell J., Shigehiko Uni, Jeffrey A. Lyon, Diane W. Taylor, Wendell Daniel, and Masamichi Aikawa. "Export of Plasmodium Falciparum Proteins to the Host Erythrocyte Membrane: Special Problems of Protein Trafficking and Topogenesis." In Host-Parasite Cellular and Molecular Interactions in Protozoal Infections, 281–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72840-2_33.

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Conference papers on the topic "Plasmodial Proteins"

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Yu, Xinran, Turgay Korkmaz, Timothy G. Lilburn, Hong Cai, Jianying Gu, and Yufeng Wang. "Heavy path mining reveals novel protein-protein associations in the malaria parasite plasmodium falciparum." In 2014 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2014. http://dx.doi.org/10.1109/bibm.2014.6999137.

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Silva, Saulo Brivaldo Mendonça da, Ana Bárbara Xavier da Silva, Mariana Souza Bezerra Cavalcanti, João Lucas Pessoa de Vasconcelos, Maria Clara Cavalcante Gomes, and Nathaly Bruna de Oliveira Silva. "A PROTEÍNA PfGARP COMO POSSÍVEL CANDIDATA À VACINA ANTIMALÁRICA." In XXVII Semana de Biomedicina Inovação e Ciência. Editora IME, 2021. http://dx.doi.org/10.51161/9786588884119/28.

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Introdução: A malária é uma parasitose que, apesar de antiga, continua sendo um grande risco para saúde pública com cerca de 445 mil mortes por ano ao redor do mundo(2). Apesar de possuir cinco agentes etiológicos, o Plasmodium falciparum é o principal, sendo responsável pelo maior número de mortes por malária(1,2). Uma vez que há diversos empecilhos quando se trata da erradicação da malária como resistência a inseticidas e a drogas antimaláricas, foi observada a necessidade de uma vacina contra o agravamento dessa parasitose(1). O fato de que a fase sanguínea do Plasmodium é atualmente apontada como um dos possíveis alvos para a ação de uma vacina, fez os pesquisadores enxergarem a proteína rica em ácido glutâmico do P. falciparum (PfGARP) que é encontrada na superfície das células vermelhas infectadas pelo parasita(2,3). Assim, fez-se necessária uma pesquisa com os anticorpos contra essa proteína para melhor elucidação. Objetivos: O objetivo deste resumo é observar os efeitos dos anticorpos anti-PfGARP contra trofozoítos do Plasmodium falciparum e como esses anticorpos oferecem proteção contra o agravamento da malária. Métodos: Foi realizada a procura nas plataformas científicas PubMed e Google Acadêmico e os artigos utilizados foram encontrados por meio do descritor “malaria vaccine”. Resultados: Os anticorpos anti-PfGARP presentes nos indivíduos estudados foram apontados como responsáveis pela diminuição da integridade morfológica dos parasitas, onde os mesmos apresentaram-se picnóticos, característicos de morte(3). Além disso, esses anticorpos causaram uma diminuição da integridade do vacúolo digestivo, apresentando-se com um tamanho menor ou até mesmo ausente(3). Outrossim, os parasitas sofreram alterações no potencial de membrana mitocondrial, tendo a mitocôndria perdido função após 24h(3). Por fim, os anticorpos anti-PfGARP ativaram a morte celular programada desses parasitas por meio da ativação de caspases(3). Conclusões: Com base no que foi exposto, é possível concluir que a PfGARP é uma excelente candidata para o desenvolvimento de uma vacina contra o Plasmodium falciparum por meio da morte dos parasitas. Sendo assim, é necessário que sejam realizados mais estudos com a PfGARP com o objetivo de obter mais informações acerca dos benefícios de uma vacina com essa proteína e, ainda, conhecer possíveis malefícios para que possa ser inclusa no mercado de forma eficaz e segura, diminuindo a ocorrência de malária grave e assim evitando o sofrimento de milhares de pessoas infectadas com esta parasitose ao redor do mundo.
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Tran, Tuan, and Chinwe Ekenna. "Protein Binding Pose Prediction via Conditional Variational Autoencoding for Plasmodium Falciparum." In 2020 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2020. http://dx.doi.org/10.1109/bibm49941.2020.9313491.

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Matos, Ada, Rodrigo Silva, Isabela Soares, Barbara Baptista, Paulo Totino, Claudio Ribeiro, Cesar Camacho, Arturo Reyes-Sandoval, Lilian Riccio, and Josué Lima Junior. "Avaliação da resposta imune humoral contra proteína TRAP (Thrombospondin-Related Adhesive Protein) de Plasmodium vivax em populações de área endêmica brasileira." In VI Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2018. http://dx.doi.org/10.35259/isi.sact.2018_27128.

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Zhao, Wei, Justin Dauwels, Jacquin Niles, and Jianshu Cao. "Deconvolution of Microarray Data Predicts Transcriptionally Regulated Protein Kinases of Plasmodium falciparum." In 2011 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2011. http://dx.doi.org/10.1109/bibm.2011.31.

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Essien, E. M., and A. L. Inyang. "CHANGES IN PLATELET SURVIVAL AND SIALIC ACID CONCENTRATION IN PLASMODIUM BERGEI INFECTED RATS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643974.

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Reduced circulating platelet count sometimes to thrombocytopenic levels in man and normally severe thrombocytopenia in animals are well known features of acute Plasmodium falciparum or experimental P. bergei infections in these respective organisms. Suggested mechanism(s), disseminated intravascular coagulation or immune mediated mechanism, thought to be involved in these observations are disputed. Shortened platelet survival has been reported in man.We now present data on platelet survival and total platelet sialic acid concentration in P. bergei-infected Wistar rats. A total of 52 rats were used. For the platelet survival studies each of the 8 suckling test animals was infected by intraperi-toneal route with mouse-passaged P. bergei 4-5 days before inaction of Cr-labelled homologous rat platelets (50 μCi Na51 CrC4/rat) the platelets being obtained from adult Wistarrats. Blood samples were then collected 2 hr after the injection (zero hr sample) and subsequently at 17.0, 42.5 and 66 hr s.Platelet recovery and survival curves were determined on these samples. It was found dat fewer platelets (as % recovery) were obtained from each infected rat sample compared with control, the difference was significant in the 42.5 and 66 hr samples: 7.9 ± 8.1 (test) vs 41.4 ± 15.2% (C) for 42.5 hr and 2.8 ±4.1 (t) vs 26.8 ± 6.2% (C) for the 66 hr samples (p < 0.005 for each). For sialic acid determinations, 40 suckling Wistar rats (30 test, 10 control) were treated as for survival studies.At identical periods, blood was collected, washed platelets obtained, lysed and protein and total sialic acid determined by Lowry (1951) and Aminoff (1961) methods respectively. Total sialic acid of 7.02 ± 4.21 nM/mg protein at 42.5 hrs and 4.8 ± 2.14 at 66 hrs were significantly less than control value of 11.43 nm/mg protein and also showed a negative correlation (r = -0.95) with % parasitaemia.It is concluded that P. bergei infection causes a reduction in total platelet sialic acid with resultant significant shortening of the platelet life span.
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Sandy, Semuel, and Irawati Wike. "Study in-silico interaction of artemisinin ligands against the wild-type Plasmodium falciparum Kelch13 protein model and the Plasmodium falciparum Kelch 13 protein model in mutations of C580Y, R539T, and F446I)." In 10TH INTERNATIONAL CONFERENCE ON APPLIED SCIENCE AND TECHNOLOGY. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0104442.

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araujo, yasmin vergani, ANDERSON MACIEL DE LIMA, ANDREIMAR MARTINS SOARES, CAROLINA BIONI GARCIA TELES, and LEONARDO DE AZEVEDO CALDERON. "CARACTERIZAÇÃO DA ATIVIDADE PLASMODICIDA DE FOSFOLIPASES BÁSICAS DO VENENO DE BOTHROPS JARARACUSSU." In II Congresso Brasileiro de Biodiversidade Virtual. Revista Multidisciplinar de Educação e meio ambiente, 2022. http://dx.doi.org/10.51189/ii-conbiv/6742.

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Introdução: A malária é uma doença negligenciada e endêmica em países subdesenvolvidos. A infecção é causada por parasitos do gênero plasmodium, anualmente, milhares de pessoas são infectadas e, muitas dessas vão ao óbito em decorrência de complicações causadas por esta patologia. Com essas informações, ressalta-se a importância da prospecção de novas biomoléculas que apresentem eficácia para o tratamento desta doença. Objetivo: O objetivo do presente trabalho foi isolar e purificar duas moléculas, sendo elas: BthTX I e II (duas fosfolipase A2 básicas) provenientes do veneno da serpente Bothrops jararacussu. Material e métodos: A purificação da PLA2 foi realizada em 2 etapas cromatográficas, sendo a primeira, cromatografia de troca iônica em resina CM-Sepharose, seguida por cromatografia de fase reversa em coluna C-18, na primeira etapa extraiu-se as frações básicas de interesse e estas foram recromatografadas em cromatografia de fase reversa. Na SDS-PAGE, foram observadas moléculas com a massa molecular aparente de 15 kDa, compatível com as fosfolipases A2 de serpentes. A atividade enzimática foi avaliada utilizando-se o substrato cromogênico 4N3OBA e demonstrou que a BthTX II é uma fosfolipase A2 enzimaticamente ativa. Em seguida, o potencial antiparasitário das proteínas isoladas foi avaliado in vitro contra formas intraeritrocíticas de Plasmodium falciparum por método de cyber green e ensaio de citotoxicidade contra as células THP-1 e HepG2 pelo método de MTT. Resultados: Os resultados de inibição antiparasitária frente a P. falciparum das PLA2 não apresentaram inibição na maior concentração testada (IC50>100 μg/mL). Ao avaliar a citotoxicidade frente às linhagens HepG2 e THP-1 observou-se que as moléculas não apresentam citotoxicidade. Os resultados do trabalho, mostram que as metodologias utilizadas para o fracionamento e purificação das moléculas foram eficazes, quanto a atividade biológica, as duas fosfolipases A2 necessitam de uma quantidade acima de (100 μg/mL) para atingirem o (IC50), quando comparado a outros resultados da literatura com moléculas de venenos de serpentes, esta concentração pode ser considerada moderadamente alta. Conclusão: Como conclusão, temos as duas proteínas básicas da fosfolipase A2, BthTX-I e BthTX-II isoladas em elevado grau de pureza, e uma alternativa para melhorar a especificidade da atividade destas moléculas, seria fazer um desenho racional de péptidos provenientes destas fosfolipases A2.
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Matos, Ada, Rodrigo Silva, Isabela Soares, Barbara Baptista, Paulo Totino, Claudio Daniel-Ribeiro, Cesar Camacho, Arturo Reyes-Sandoval, Lilian Pratt-Riccio, and Josué Lima Junior. "Evaluation of humoral response of individuals naturally exposed to malaria against synthetic and recombinant antigens representing Plasmodium vivax TRAP protein." In IV International Symposium on Immunobiologicals & VII Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2019. http://dx.doi.org/10.35259/isi.sact.2019_32533.

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Silva, Rodrigo, Isabela Soares, Danielly Sequeira, Paula Luca, João Silva, Joseli Ferreira, and Josué Lima Junior. "PvMSP9E795-V808: antigenicidade e imunogenicidade do epítopo de célula-B identificado in silico na proteína-9 de superfície de merozoítas de plasmodium vivax." In III Seminário Anual Científico e Tecnológico de Bio-Manguinhos. Instituto de Tecnologia em Imunobiológicos, 2016. http://dx.doi.org/10.35259/isi.sact.2016_27315.

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Reports on the topic "Plasmodial Proteins"

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Angov, Evelina. Production of a Recombinant E. coli Expressed Malarial Vaccine from the C-Terminal Fragment of Plasmodium Falciparum 3D7 Merozoite Surface Protein-1. Fort Belvoir, VA: Defense Technical Information Center, September 2000. http://dx.doi.org/10.21236/ada391249.

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