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Formation of the food vacuole in Plasmodium falciparum: A potential role for the 19 kDa fragment of merozoite surface protein 1 (MSP119)


Reference:

Dluzewski, A. R., Ling, I. T., Hopkins, J. M., Grainger, M., Margos, G., Mitchell, G. H., Holder, A. A. and Bannister, L. H., 2008. Formation of the food vacuole in Plasmodium falciparum: A potential role for the 19 kDa fragment of merozoite surface protein 1 (MSP119). PLoS ONE, 3 (8), e3085.

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http://dx.doi.org/10.1371/journal.pone.0003085

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Abstract

Plasmodium falciparum Merozoite Surface Protein 1 (MSP1) is synthesized during schizogony as a 195-kDa precursor that is processed into four fragments on the parasite surface. Following a second proteolytic cleavage during merozoite invasion of the red blood cell, most of the protein is shed from the surface except for the C-terminal 19-kDa fragment (MSP119), which is still attached to the merozoite via its GPI-anchor. We have examined the fate of MSP119 during the parasite's subsequent intracellular development using immunochemical analysis of metabolically labeled MSP119, fluorescence imaging, and immuno-electronmicroscopy. Our data show that MSP119 remains intact and persists to the end of the intracellular cycle. This protein is the first marker for the biogenesis of the food vacuole; it is rapidly endocytosed into small vacuoles in the ring stage, which coalesce to form the single food vacuole containing hemozoin, and persists into the discarded residual body. The food vacuole is marked by the presence of both MSP119 and the chloroquine resistance transporter (CRT) as components of the vacuolar membrane. Newly synthesized MSP1 is excluded from the vacuole. This behavior indicates that MSP119 does not simply follow a classical lysosome-like clearance pathway, instead, it may play a significant role in the biogenesis and function of the food vacuole throughout the intra-erythrocytic phase.

Details

Item Type Articles
CreatorsDluzewski, A. R., Ling, I. T., Hopkins, J. M., Grainger, M., Margos, G., Mitchell, G. H., Holder, A. A. and Bannister, L. H.
DOI10.1371/journal.pone.0003085
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URLURL Type
http://dx.doi.org/10.1371/journal.pone.0003085Free Full-text
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code28624

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