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Glycobiology Advance Access originally published online on December 17, 2002
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Glycobiology, 2003, Vol. 13, No. 5 351-361
© 2003 Oxford University Press

Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes

Mitali Chatterjee1,3, Anil Kumar Chava1,3, Guido Kohla4, Santanu Pal3, Anette Merling5, Stephan Hinderlich6, Ulrike Unger7, Peter Strasser7, Gerrit J. Gerwig8, Johannis P. Kamerling8, Reinhard Vlasak7, Paul R. Crocker9, Roland Schauer4, Reinhard Schwartz-Albiez5 and Chitra Mandal23

3 Immunobiology Division, Indian Institute of Chemical Biology, 4, Raja S. C. Mullick Road, Calcutta 700032, India
4 Biochemisches Institut, Christian-albrechts-universität Zu Kiel, Olshausenstr. 40, D-24098 Kiel, Germany
5 Schwerpunkt Tumorimmunologie, Deutsches Krebsforschungszentrum, Heidelberg, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
6 Institut Für Molekularbiologie Und Biochemie Freie Universität Berlin, Arnimallee 22, D-14195 Berlin-dahlem, Germany
7 Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstr. 11, A-5020 Salzburg, Austria
8 Bijvoet Center for Biomolecular Research, Department of Bio-organic Chemistry, Utrecht University, P.O. Box 80075, NL-3508 TB Utrecht, The Netherlands
9 Wellcome Trust Biocentre, Division of Cell Biology and Immunology, School of Life Sciences, Dundee University, Dundee DD1 5EH, UK

Received on September 19, 2002; revised on October 31, 2002; accepted on November 4, 2002

Sialic acids as terminal residues of oligosaccharide chains play a crucial role in several cellular recognition events. The presence of sialic acid on promastigotes of Leishmania donovani, the causative organism of Indian visceral leishmaniasis, was demonstrated by fluorimetric high-performance liquid chromatography showing Neu5Ac and, to a minor extent, Neu5,9Ac2. The presence of Neu5Ac was confirmed by GC/MS analysis. Furthermore, binding with sialic acid-binding lectins Sambucus nigra agglutinin (SNA), Maackia amurensis agglutinin (MAA), and Siglecs showed the presence of both {alpha}2,3- and {alpha}2,6-linked sialic acids. No endogenous biosynthetic machinery for Neu5Ac could be demonstrated in the parasite. Concomitant western blotting of parasite membranes and culture medium with SNA demonstrated the presence of common sialoglyconjugates (123, 90, and 70 kDa). Similarly, binding of MAA with parasite membrane and culture medium showed three analogous sialoglycans corresponding to 130, 117, and 70 kDa, indicating that {alpha}2,3- and {alpha}2,6-linked sialoglycans are adsorbed from the fetal calf serum present in the culture medium. L. donovani promastigotes also reacted with Achatinin-H, a lectin that preferentially identifies 9-O-acetylated sialic acid in {alpha}2->6 GalNAc linkage. This determinant was evidenced on parasite cell surfaces by cell agglutination, ELISA, and flow cytometry, where its binding was abolished by pretreatment of cells with a recombinant 9-O-acetylesterase derived from the HE1 region of the influenza C esterase gene. Additionally, binding of CD60b, a 9-O-acetyl GD3-specific monoclonal antibody, corroborated the presence of terminal 9-O-acetylated disialoglycans. Our results indicate that sialic acids ({alpha}2->6 and {alpha}2->3 linked) and 9-O-acetyl derivatives constitute components of the parasite cell surface.

1 These authors contributed equally to this work.

2 To whom correspondence should be addressed; e-mail: cmandal{at}iicb.res.in


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