Leishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment

Adrien Weingärtner, Gerdi Christine Kemmer, Frederic D. Müller, Ricardo Andrade Zampieri, Jürgen Schiller, Thomas Günther-Pomorski

    52 Citations (Scopus)
    1941 Downloads (Pure)

    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 31P 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.

    Original languageEnglish
    JournalP L o S One
    Volume7
    Issue number8
    Number of pages11
    ISSN1932-6203
    DOIs
    Publication statusPublished - 1 Aug 2012

    Fingerprint

    Dive into the research topics of 'Leishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment'. Together they form a unique fingerprint.

    Cite this