Premium
Proteases and chaperones are the most abundant proteins in the parasitophorous vacuole of Plasmodium falciparum ‐infected erythrocytes
Author(s) -
Nyalwidhe Julius,
Lingelbach Klaus
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500379
Subject(s) - vacuole , proteases , plasmodium falciparum , cytosol , microbiology and biotechnology , biology , proteome , cellular compartment , organelle , cytoplasm , parasite hosting , protein targeting , biochemistry , biotinylation , proteomics , plasmodium (life cycle) , membrane protein , enzyme , cell , malaria , gene , immunology , membrane , world wide web , computer science
After invasion of erythrocytes, the human malaria parasite Plasmodium falciparum resides within a parasitophorous vacuole (PV) which forms an interface between the host cell cytosol and the parasite surface. This vacuole protects the parasite from potentially harmful substances, but allows access of essential nutrients to the parasite. Furthermore, the vacuole acts as a transit compartment for parasite proteins en route to the host cell cytoplasm. Recently we developed a strategy to biotin label soluble proteins of the PV. Here, we have paired this strategy with a high‐throughput MALDI‐TOF‐MS analysis to identify 27 vacuolar proteins. These proteins fall into the following main classes: chaperones, proteases, and metabolic enzymes, consistent with the expected functions of the vacuole. These proteins are likely to be involved in several processes including nutrient acquisition from the host cytosol, protein sorting within the vacuole, and release of parasites at the end of the intraerythrocytic cycle.