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Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes

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Title Identification and characterization of adsorbed serum sialoglycans on
Leishmania donovani promastigotes
 
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
 
Subject Infectious Diseases and Immunology
 
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.
 
Publisher Oxford University Press
 
Date 2003
 
Type Article
PeerReviewed
 
Format application/pdf
 
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.
 
Relation http://dx.doi.org/10.1093/glycob/cwg027
http://www.eprints.iicb.res.in/598/