Show simple item record

dc.contributor.authorWeingärtner, Adrien
dc.contributor.authorKemmer, Gerdi
dc.contributor.authorMüller, Frederic D
dc.contributor.authorZampieri, Ricardo Andrade
dc.contributor.authorGonzaga dos Santos, Marcos
dc.contributor.authorSchiller, Jürgen
dc.contributor.authorPomorski, Thomas Günther
dc.date.accessioned2013-02-21T09:09:40Z
dc.date.available2013-02-21T09:09:40Z
dc.date.issued2012
dc.identifier.citationLeishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment. 2012, 7 (8):e42070 PLoS ONEen_GB
dc.identifier.issn1932-6203
dc.identifier.pmid22870283
dc.identifier.doi10.1371/journal.pone.0042070
dc.identifier.urihttp://hdl.handle.net/10033/269913
dc.description.abstractThe 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.
dc.language.isoenen
dc.rightsArchived with thanks to PloS oneen_GB
dc.subject.meshAnnexin A5en_GB
dc.subject.meshAntiprotozoal Agentsen_GB
dc.subject.meshCell Membrane Permeabilityen_GB
dc.subject.meshHumansen_GB
dc.subject.meshLeishmaniaen_GB
dc.subject.meshPhagocytosisen_GB
dc.subject.meshPhosphatidylserinesen_GB
dc.subject.meshPhosphorylcholineen_GB
dc.titleLeishmania promastigotes lack phosphatidylserine but bind annexin V upon permeabilization or miltefosine treatment.en
dc.typeArticleen
dc.contributor.departmentInstitute of Biology, Humboldt-Universität zu Berlin, Berlin, Germany.en_GB
dc.identifier.journalPloS oneen_GB
refterms.dateFOA2018-06-12T23:47:03Z
html.description.abstractThe 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.


Files in this item

Thumbnail
Name:
weingärtner et al_final.pdf
Size:
824.0Kb
Format:
PDF
Description:
Open Access publication

This item appears in the following Collection(s)

Show simple item record