Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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Title |
Identification and characterization of adsorbed serum sialoglycans on
Leishmania donovani promastigotes
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Creator |
Chatterjee, Mitali
Chava, Anil Kumar Kohla, Guido Pal, Santanu Merling, Anette Hinderlich, Stephan Unger, Ulrike Strasser, Peter Gerwig, Gerrit J Kamerling, Johannis P Vlasak, Reinhard Crocker, Paul R Schauer, Roland Schwartz-Albiez, Reinhard Mandal, Chitra |
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Subject |
Infectious Diseases and Immunology
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Description |
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 leishmani-
asis, 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 a2,3- and a2,6-linked sialic acids. No endo-
genous biosynthetic machinery for Neu5Ac could be demon-
strated in the parasite. Concomitant western blotting of
parasite membranes and culture medium with SNA demon-
strated the presence of common sialoglyconjugates (123, 90,
and 70 kDa). Similarly, binding of MAA with parasite mem-
brane and culture medium showed three analogous sialogly-
cans corresponding to 130, 117, and 70 kDa, indicating that
a2,3- and a2,6-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 a2!6
GalNAc linkage. This determinant was evidenced on parasite
cell surfaces by cell agglutination, ELISA, and flow cytome-
try, 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 disialo-
glycans. Our results indicate that sialic acids (a2!6 and
a2!3 linked) and 9-O-acetyl derivatives constitute compo-
nents of the parasite cell surface.
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Publisher |
Oxford University Press
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Date |
2003
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://www.eprints.iicb.res.in/598/1/GLYCOBIOLOGY%2C_13(_5)%2C_351%2D361[67].pdf
Chatterjee, Mitali and Chava, Anil Kumar and Kohla, Guido and Pal, Santanu and Merling, Anette and Hinderlich, Stephan and Unger, Ulrike and Strasser, Peter and Gerwig, Gerrit J and Kamerling, Johannis P and Vlasak, Reinhard and Crocker, Paul R and Schauer, Roland and Schwartz-Albiez, Reinhard and Mandal, Chitra (2003) Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes. Glycobiology, 13 (5). pp. 351-361. |
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Relation |
http://dx.doi.org/10.1093/glycob/cwg027
http://www.eprints.iicb.res.in/598/ |
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