Glycobiology Advance Access published online on June 9, 2004
Glycobiology, doi:10.1093/glycob/cwh111
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1 Immunobiology Division, Indian Institute of Chemical Biology, 4, Raja S. C. Mullick Road, Kolkata 700032, India
* To whom correspondence should be addressed. E-mail: cmandal{at}iicb.res.in; Chitra_mandal@yahoo.com.
Sialic acids as terminal residues of oligosaccharide chains play crucial roles in several cellular recognition events. Exploiting the selective affinity of Achatinin-H towards N-acetyl-9-O-acetylneuraminic acid-
Revised June 3, 2004
Accepted June 6, 2004
ORIGINAL ARTICLES
Purification and characterisation of 9-O-acetylated sialoglycoproteins from leukaemic cells and their potential as immunological tool for monitoring childhood acute lymphoblastic leukaemia
2 Drug Design Development and Molecular Modelling, Indian Institute of Chemical Biology, 4, Raja S. C. Mullick Road, Kolkata 700032, India
3 Biochemisches Institut, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, D-24098 Kiel, Germany
4 Biochemistry Center, Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
5 Schwerpunkt Tumorimmunologie, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
6 Vivekananda Institute of Medical Sciences, Kolkata 700045, India
Abstract 
2-6-GalNAc, we have demonstrated the presence of 9-O-acetylated sialoglycoproteins (Neu5,9Ac2-GPs) on lymphoblasts of seventy children with acute lymphoblastic leukaemia (ALL) and on leukaemic cell lines by fluorimetric HPLC and flow cytometric analysis. This study aims to assess the structural aspect of the glycotope of Neu5,9Ac2-GPsALL and to evaluate whether these disease-specific molecules can be used to monitor the clinical outcome of ALL. The Neu5,9Ac2-GPsALL were affinity-purified and three distinct leukaemia-specific molecular determinants (135, 120 and 90 kDa) were demonstrated by SDS-PAGE, Western blotting and isoelectric focusing. The carbohydrate epitope of Neu5,9Ac2-GPsALL was confirmed by using synthetic sialic acid analogues. The enhanced presence of anti-Neu5,9Ac2-GPALL antibody in ALL patients prompted us to develop an Antigen-ELISA using purified Neu5,9Ac2-GPsALL as coating antigens. Purified antigen was able to detect leukaemia-specific antibodies at presentation of disease, which gradually decreased with treatment. Longitudinal monitoring of 18 patients revealed that in the early phase of the treatment patients with lower anti-Neu5,9Ac2-GPs showed a better prognosis. Minimal cross reactivity was observed in other haematological disorders (n = 50) like chronic myeloid leukaemia, acute myelogenous leukaemia, chronic lymphocytic leukaemia, and non-Hodgkin's lymphoma as well as normal healthy individuals (n = 21). This study demonstrated the potential of purified Neu5,9Ac2-GPsALL, as an alternate tool, for detection of anti-Neu5,9Ac2-GP antibodies to be helpful for diagnosis and monitoring of childhood ALL patients.
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