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Leishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment.
Weingärtner, Adrien Kemmer, Gerdi Müller, Frederic D Zampieri, Ricardo Andrade Gonzaga dos Santos, Marcos Schiller, Jürgen Pomorski, Thomas Günther
Weingärtner, Adrien
Kemmer, Gerdi
Müller, Frederic D
Zampieri, Ricardo Andrade
Gonzaga dos Santos, Marcos
Schiller, Jürgen
Pomorski, Thomas Günther
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Abstract
The protozoan parasite Leishmania is an intracellular pathogen infecting and replicating inside vertebrate host macrophages. A recent model suggests that promastigote and amastigote forms of the parasite mimic mammalian apoptotic cells by exposing phosphatidylserine (PS) at the cell surface to trigger their phagocytic uptake into host macrophages. PS presentation at the cell surface is typically analyzed using fluorescence-labeled annexin V. Here we show that Leishmania promastigotes can be stained by fluorescence-labeled annexin V upon permeabilization or miltefosine treatment. However, combined lipid analysis by thin-layer chromatography, mass spectrometry and (31)P nuclear magnetic resonance (NMR) spectroscopy revealed that Leishmania promastigotes lack any detectable amount of PS. Instead, we identified several other phospholipid classes such phosphatidic acid, phosphatidylethanolamine; phosphatidylglycerol and phosphatidylinositol as candidate lipids enabling annexin V staining.
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Leishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment. 2012, 7 (8):e42070 PLoS ONE
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en
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1932-6203
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