Immunoelectron Microscopy of Parasites

Aikawa, Masamichi; Atkinson, Carter T.

doi:10.1016/s0065-308x(08)60106-2

Cited by 65 publications

(28 citation statements)

References 184 publications

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“…[5][6][7][8][9] Our previous [1][2][3] and present data support these findings. In the case of human malaria, CD36 antigens (sequestrin) on erythrocytes are known to mediate adherence and subsequent infection of Plasmodium falciparum.…”

Section: Discussionsupporting

confidence: 89%

Protection against malaria by anti‐erythropoietin antibody due to suppression of erythropoiesis in the liver and at other sites

et al. 2005

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SummaryWe have previously reported that erythropoiesis commences in the liver and spleen after malarial infection, and that newly generated erythrocytes in the liver are essential for infection of malarial parasites as well as continuation of infection. At this time, erythropoietin (EPO) is elevated in the serum. In the present study, we administered EPO or anti-EPO antibody into C57BL/6 (B6) mice to modulate the serum level of EPO. When mice were infected with a non-lethal strain (17NXL) of Plasmodium yoelii (blood-stage infection of 10 4 parasitized erythrocytes per mouse), parasitemia continued for 1 month, showing a peak at day 17. Daily injection of EPO (200 IU/day per mouse) from day five to day 14 prolonged parasitemia, whereas injection of anti-EPO antibody (1.5 mg/day per mouse) every second day from day five to day 28 decreased it. Erythropoiesis was confirmed in the liver, spleen and bone marrow by the appearance of nucleated erythrocytes (TER119+). When anti-EPO antibody was injected by the same protocol into mice infected with a lethal strain (17XL) of P. yoelii , all mice showed decreased parasitemia and recovered from the infection. These results suggest that the use of anti-EPO antibody after malarial infection may be of therapeutic value in severe cases of malaria.

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Section: Discussionsupporting

confidence: 89%

Protection against malaria by anti‐erythropoietin antibody due to suppression of erythropoiesis in the liver and at other sites

et al. 2005

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“…Whether or not such difference is related to distinct biological properties is unknown, but may reflect differences in their development. Analogy can be made with works on human plasmodia (Aikawa & Atkinson 1990, Rey 1991, Bannister et al 2000, where it has been described that the processes of shizogony occurring in the vertebrate host yield exoerythrocytic merozoites and erythrocyte merozoites with similar biological capacities, but with partly different morphologies and antigenicities. Thus, it is tempting to speculate that the IMA may be the parasitological equivalent to exoerythrocytic merozoites derived from infective sporozites transmitted by the vector insect, while the ITA may be equivalent to the erythrocyte merozoites.…”

Section: Discussionmentioning

confidence: 96%

Morphological comparison of axenic amastigogenesis of trypomastigotes and metacyclic forms of Trypanosoma cruzi

Navarro

Lima

Askue

et al. 2003

Mem. Inst. Oswaldo Cruz

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“…Fixed samples were washed, dehydrated and embedded in LR White resin (Polysciences, Inc.). Thin sections (70 -80 nm) were blocked in a phosphate buffer containing 5% w/v nonfat dry milk and 0.01% v/v Tween 20 (21). Grids were incubated at 4°C overnight in solutions containing variable concentrations of rabbit antiserum reactive to domain-specific recombinant proteins diluted in the blocking buffer.…”

Section: Methodsmentioning

confidence: 99%

Stage-dependent Localization of a Novel Gene Product of the Malaria Parasite, Plasmodium falciparum

Nguyên¹,

Fujioka²,

Kang³

et al. 2001

Journal of Biological Chemistry

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A novel Plasmodium falciparum gene, MB2, was identified by screening a sporozoite cDNA library with the serum of a human volunteer protected experimentally by the bites of P. falciparum-infected and irradiated mosquitoes. The single-exon, single-copy MB2 gene is predicted to encode a protein with an M r of 187,000. The MB2 protein has an amino-terminal basic domain, a central acidic domain, and a carboxyl-terminal domain with similarity to the GTP-binding domain of the prokaryotic translation initiation factor 2. MB2 is expressed in sporozoites, the liver, and blood-stage parasites and gametocytes. The MB2 protein is distributed as a ϳ120-kDa moiety on the surface of sporozoites and is imported into the nucleus of blood-stage parasites as a ϳ66-kDa species. Proteolytic processing is favored as the mechanism regulating the distinct subcellular localization of the MB2 protein. This differential localization provides multiple opportunities to exploit the MB2 gene product as a vaccine or therapeutic target.

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Immunoelectron Microscopy of Parasites

Cited by 65 publications

References 184 publications

Protection against malaria by anti‐erythropoietin antibody due to suppression of erythropoiesis in the liver and at other sites

Protection against malaria by anti‐erythropoietin antibody due to suppression of erythropoiesis in the liver and at other sites

Morphological comparison of axenic amastigogenesis of trypomastigotes and metacyclic forms of Trypanosoma cruzi

Stage-dependent Localization of a Novel Gene Product of the Malaria Parasite, Plasmodium falciparum

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