Immunoprecipitation of [
            <sup>3</sup>
            H]Dihydroartemisinin Translationally Controlled Tumor Protein (TCTP) Adducts from
            <i>Plasmodium falciparum</i>
            -Infected Erythrocytes by Using Anti-TCTP Antibodies

Bhisutthibhan, Jamaree; Meshnick, Steven R.

doi:10.1128/aac.45.8.2397-2399.2001

Cited by 55 publications

(41 citation statements)

References 34 publications

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“…Based on densitometric scanning of this band, it was estimated that the schistosomula of S. mansoni secrete approximately 1 g of SmTCTP/1000 schistosomula. As has been reported previously with other TCTP proteins (10,14,15), the SmTCTP antibody also recognized several proteins most prominently around 25, 60, 85, and 150 kDa in molecular size in the worm homogenates of schistosomula, adult male worms, and adult female worms (Fig. 4).…”

Section: Resultsmentioning

confidence: 48%

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Rao¹,

Chen

Munirathinam

et al. 2002

Journal of Biological Chemistry

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A homologue of the mammalian translationally controlled tumor protein (TCTP) was cloned from the human parasite Schistosoma mansoni (SmTCTP). Sequence analysis showed that SmTCTP differed from other reported TCTPs in having only one signature sequence. Subsequently, SmTCTP was cloned in a T7 expression system and expressed as a histidine-tagged fusion protein. Recombinant SmTCTP (rSmTCTP) has a molecular mass of ϳ23 kDa with the histidine tag. Further analysis showed that SmTCTP transcripts and protein are expressed in all life cycle stages of the parasite within the vertebrate hosts. Interestingly, antibodies to SmTCTP were present in the sera of mice 9 weeks after infection with S. mansoni. Characterization studies showed that rSmTCTP is a calcium-binding protein that can cause histamine release from basophil/mast cells and induce eosinophil infiltration. These findings suggest that SmTCTP may have an important role in the development of allergic inflammatory responses associated with schistosomiasis and may be a target for new drug development.

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Section: Resultsmentioning

confidence: 48%

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Rao¹,

Chen

Munirathinam

et al. 2002

Journal of Biological Chemistry

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“…22) These intermediates interfere with the heme detoxification process and form adducts with the multiple parasitic proteins such as the P. falciparum translationally controlled tumor protein (PfTCTP) and sarco/endoplasmic reticulum Ca 2+ -ATPase (SERCA). [23][24][25] The source of heme for activation of artemisinin is controversial. During hemoglobin digestion process in food vacuole, the ferrous heme could be generated transiently and react with artemisinin intracellularly before it is oxidized to ferric heme.…”

Section: Discussionmentioning

confidence: 99%

Extracellular Heme Enhances the Antimalarial Activity of Artemisinin

Tangnitipong

Thaptimthong

Srihirun

et al. 2012

Biological & Pharmaceutical Bulletin

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Artemisinin exerts the antimalarial activity through activation by heme. The hemolysis in malaria results in the elevated levels of plasma heme which may affect the activity of artemisinin. We hypothesized that the extracellular heme would potentiate the antimalarial activity of artemisinin. Hemin (ferric heme) at the pathologic concentrations enhanced the activity of artemisinin against Plasmodium falciparum in vitro and increased the levels of the lipid peroxidation products in the presence of artemisinin. The antimalarial activity of artemisinin and potentiation by hemin was decreased by vitamin E. Hemin had no effect on the activity of quinoline drugs (chloroquine, quinine and mefloquine). Furthermore, the oxidative effect of hemin in the presence of artemisinin or quinoline drugs was studied using low-density lipoprotein (LDL) oxidation as a model. Artemisinin enhanced the effects of hemin on lipid peroxidation and a decrease of tryptophan fluorescence in LDL whereas the quinoline drugs inhibited the oxidation by hemin. In conclusion, the extracellular hemin enhances the antimalarial activity of artemisinin as a result of the increasing oxidative effect of hemin.

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“…27 Also this antigen is known to be bound to some anti-malarial and anticancer drugs. 8,9 A purified antigen was prepared using immunoblotting for the diagnosis of nocardiosis with a specific immunodominant antibody and it was found to be useful. 11 This method was also used for diagnosis of chromoblastomycosis, and characterisation of Fonsecaea pedrosoi antigens.…”

Section: Discussionmentioning

confidence: 99%

“…[5][6][7] Management of mycetoma depends on correct diagnosis of the causative organism, extent of the disease and its spread along the different tissue planes. 8,9 Imaging, cytological, histopathological, phenotypic, molecular, culture and serological diagnostic techniques are available to achieve that. [10][11][12][13][14][15][16] However, these tools are tedious, invasive, expensive and may not be available in areas endemic for mycetoma.…”

Section: Introductionmentioning

confidence: 99%

Use of immunoblotting in testingMadurella mycetomatisspecific antigen

Elbadawi¹,

Mahgoub

Mahmoud³

et al. 2016

Trans R Soc Trop Med Hyg

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Background: Though serodiagnosis of actinomycetoma is established, that of eumycetoma due to Madurella mycetomatis is limited because of lack of pure antigen. Reliable rapid tests are needed to make an accurate timely diagnosis. The purpose of this study is to detect antigen parts of M. mycetomatis, which act specifically with M. mycetomatis antibodies.Methods: Cytoplasmic antigen was prepared from molecularly identified cultures of M. mycetomatis by sonication, ultracentrifugation, dried, weighed and appropriately reconstituted. M. mycetomatis cytoplasmic antigen were separated using 12% sodium dodecyl sulfate-polyacrylamide gel, and immunoblotting to detect the reactive ones.Immunoblotting was carried out in nitrocellulose strips containing different molecular size. Sera from patients and co-patients as control were used.Results: When stained with Coomassie brilliant blue R 250 seven molecular weights appeared but only three, 45, 60, 95 kDa reacted with M. mycetomatis patients few from control group, one from a malaria patient. No reactive band was observed with sera from actinomycetoma, Aspergillus flavus-associated aspergillosis, schistosomiasis, leishmaniasis, fungal sinusitis nor healthy controls.Conclusions: Specific fractions of M. mycetomatis antigen which were demonstrated by immunoblotting showed 75% sensitivity and 95% specificity. The true negative tests were 14 patients (32.5%). This also means that immunoblotting is reasonably reliable in diagnosis and follow-up of eumycetoma patients.

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Immunoprecipitation of [ ³ H]Dihydroartemisinin Translationally Controlled Tumor Protein (TCTP) Adducts from Plasmodium falciparum -Infected Erythrocytes by Using Anti-TCTP Antibodies

Cited by 55 publications

References 34 publications

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Extracellular Heme Enhances the Antimalarial Activity of Artemisinin

Use of immunoblotting in testingMadurella mycetomatisspecific antigen

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Immunoprecipitation of [ 3 H]Dihydroartemisinin Translationally Controlled Tumor Protein (TCTP) Adducts from Plasmodium falciparum -Infected Erythrocytes by Using Anti-TCTP Antibodies

Cited by 55 publications

References 34 publications

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Cloning and Characterization of a Calcium-binding, Histamine-releasing Protein from Schistosoma mansoni

Extracellular Heme Enhances the Antimalarial Activity of Artemisinin

Use of immunoblotting in testingMadurella mycetomatisspecific antigen

Contact Info

Product

Resources

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Immunoprecipitation of [ ³ H]Dihydroartemisinin Translationally Controlled Tumor Protein (TCTP) Adducts from Plasmodium falciparum -Infected Erythrocytes by Using Anti-TCTP Antibodies