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Cationic detergents enable the separation of membrane proteins of Plasmodium falciparum ‐infected erythrocytes by 2D gel electrophoresis
Author(s) -
Philipp Stephan,
Jakoby Thomas,
Tholey Andreas,
Janssen Ottmar,
Leippe Matthias,
Gelhaus Christoph
Publication year - 2012
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100520
Subject(s) - plasmodium falciparum , membrane protein , red blood cell , membrane , biology , parasite hosting , gel electrophoresis , cell , plasmodium (life cycle) , microbiology and biotechnology , biochemistry , cell membrane , chemistry , malaria , immunology , world wide web , computer science
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.