Detection and species determination of malaria parasites by PCR: Comparison with microscopy and with ParaSight-F and ICT Malaria Pf tests in a clinical environment

Journal of Clinical Microbiology3751269-1273JCMI

Direct PCR amplification and sequence analysis of extrachromosomal Plasmodium DNA from dried blood spots

10.1016/S0001-706X(97)00080-6Acta Tropica681105-114ACTR

Resonance Raman microspectroscopy of normal erythrocytes and Plasmodium berghei-infected erythrocytes

10.1366/0003702991947874Applied Spectroscopy5391097-1101APSP

Identification of a Plasmodium berghei antigen sharing common features with P. Falciparum and P. Chabaudi parasitophorous-vacuole membrane antigens

10.1007/s004360050083Parasitology Research822130-135PARR

Raman microspectroscopy of normal erythrocytes and plasmodium berghei-infected erythrocytes

10.1366/000370202760295340Applied Spectroscopy5691126-1131APSP

Partial nucleotide sequence and organisation of extrachromosomal plastid-like DNA in Plasmodium berghei

10.1016/S0378-1119(97)00385-5Gene2001-291-98GENE

etramps, a New Plasmodium falciparum Gene Family Coding for Developmentally Regulated and Highly Charged Membrane Proteins Located at the Parasite–Host Cell Interface

After invasion of erythrocytes, the human malaria parasite Plasmodium falciparum resides within a parasitophorous vacuole and develops from morphologically and metabolically distinct ring to trophozoite stages. During these developmental phases, major structural changes occur within the erythrocyte, but neither the molecular events governing this development nor the molecular composition of the parasitophorous vacuole membrane (PVM) is well known. Herein, we describe a new family of highly cationic proteins from P. falciparum termed early transcribed membrane proteins (ETRAMPs). Thirteen members were identified sharing a conserved structure, of which six were found only during ring stages as judged from Northern and Western analysis. Other members showed different stage-specific expression patterns. Furthermore, ETRAMPs were associated with the membrane fractions in Western blots, and colocalization and selective permeabilization studies demonstrated that ETRAMPs were located in the PVM. This was confirmed by immunoelectron microscopy where the PVM and tubovesicular extensions of the PVM were labeled. Early expressed ETRAMPs clearly defined separate PVM domains compared with the negatively charged integral PVM protein EXP-1, suggesting functionally different domains in the PVM with an oppositely charged surface coat. We also show that the dynamic change of ETRAMP composition in the PVM coincides with the morphological changes during development. The P. falciparum PVM is an important structure for parasite survival, and its analysis might provide better understanding of the requirements of intracellular parasites