Pinero T, Peres VJ, Katzin A, Couto AS Metabolic oligosaccharide engineering of Plasmodium falciparum intraerythrocytic stages allows direct glycolipid analysis by mass spectrometry Molecular and Biochemical Parasitology182(1-2) (2012)
88-92
/Variants 0/-+ Ste-(1-1)-+
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Subst-(1-2)-EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-L-myoIno-(1--P--3)--Gro
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Ste-(1-2)-+
/Variants 0/ is:
90%Pam-(1-2)-
OR (exclusively)
10%Myr-(1-2)-
Subst = protein
NCBI PubMed ID:22245334 Publication DOI:10.1016/j.molbiopara.2011.12.008 Journal NLM ID:8006324 Correspondence: Couto A.S. <acoutoqo.fcen.uba.ar> Institutions: CIHIDECAR, Departamento de Química Orgánica, Pabellón II, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina, Departamento de Parasitología, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
A recent addition to the arsenal of tools for glycome analysis is the use of metabolic labels that allow covalent tagging of glycans with imaging probes. In this work we show that N-azidoglucosamine was successfully incorporated into glycolipidic structures of Plasmodium falciparum intraerythrocytic stages. The ability to tag glycoconjugates selectively with a fluorescent reporter group permits TLC detection of the glycolipids providing a new method to quantify dynamic changes in the glycosylation pattern and facilitating direct mass spectrometry analyses. Presence of glycosylphosphatidylinositol and glycosphingolipid structures was determined in the different extracts. Furthermore, the fluorescent tag was used as internal matrix for the MALDI experiment making even easier the analysis.
mass spectrometry, glycolipids, Glycosylphosphatidylinositol, Plasmodium, metabolic oligosaccharide engineering, P.falciparum
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