Abstract |
The intraerythrocytic stage of Plasmodium falciparum alters the characteristics of its host cell by exporting selected plasmodial proteins. Although it is clear that the physicochemical and immunobiological properties of the host cell are modulated during parasite development, the involved plasmodial proteins and their mode of action are not completely known. Using cetyltrimethylammonium bromide ( CTAB) or benzyldimethyl-n-hexadecylammonium chloride (16-BAC) for the first dimension and SDS for the second dimension, we separated proteins from membranes of human erythrocytes and of erythrocytes infected with the malaria parasite P. falciparum. Protein spots were analyzed by MALDI-TOF/TOF MS and annotated in respective 2D master gels. By using the alternative 2D approach, characteristic host cell membrane proteins and, more importantly, membrane-associated and exported plasmodial proteins were identified that might play a role in parasite-induced host cell modulation.
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Authors | Stephan Philipp, Thomas Jakoby, Andreas Tholey, Ottmar Janssen, Matthias Leippe, Christoph Gelhaus |
Journal | Electrophoresis
(Electrophoresis)
Vol. 33
Issue 7
Pg. 1120-8
(Apr 2012)
ISSN: 1522-2683 [Electronic] Germany |
PMID | 22539315
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
Chemical References |
- Cetrimonium Compounds
- Detergents
- Fatty Alcohols
- Membrane Proteins
- Protozoan Proteins
- Quaternary Ammonium Compounds
- cetalkonium chloride
- Cetrimonium
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Topics |
- Cetrimonium
- Cetrimonium Compounds
(chemistry)
- Detergents
(chemistry)
- Electrophoresis, Gel, Two-Dimensional
- Erythrocyte Membrane
(chemistry, parasitology)
- Fatty Alcohols
(chemistry)
- Host-Parasite Interactions
- Humans
- Malaria, Falciparum
(metabolism)
- Membrane Proteins
(analysis, chemistry)
- Plasmodium falciparum
(metabolism)
- Proteomics
(methods)
- Protozoan Proteins
(analysis, chemistry)
- Quaternary Ammonium Compounds
(chemistry)
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