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Glycobiology Advance Access published online on July 25, 2007
Glycobiology, doi:10.1093/glycob/cwm077
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Structural basis for recognition of breast and colon cancer epitopes Tn antigen and Forssman disaccharide by Helix pomatia lectin

Julien Lescar2,3,4, Jean-Frederic Sanchez2,4, Aymeric Audfray4, Jean-Luc Coll5, Christelle Breton4, Edward P Mitchell1,6 and Anne Imberty1,4

4 Centre de Recherches sur les Macromolécules Végétales, CNRS (affiliated with Université Joseph Fourier), BP53, 38041 Grenoble cedex 09, France
5 INSERM, U823, Cibles Diagnostiques ou Thérapeutiques et Vectorisation des Drogues dans le Cancer du Poumon Institut Albert Bonniot, 38706 La Tronche
6 E.S.R.F. Experiments Division, BP 220, F-38043, Grenoble Cedex, France

1 To whom correspondence should be addressed; email: Mitchell{at}esrf.fr or imberty{at}cermav.cnrs.fr

Received on April 10, 2007; accepted on July 10, 2007

Helix pomatia agglutinin (HPA) is a lectin that has been used extensively in histopathology since its binding to tissue sections from breast and colon cancers is correlated with the worst prognosis for the patients. The lectin recognizes {alpha}-D-N-acetylgalactosamine ({alpha}GalNAc) containing epitopes which are only present in cancer cell lines having a high likelihood to undergo metastasis, such as the HT29 cancer colon cell line. Several breast cancer cell lines have also been shown to be labeled, although IGROV1, an ovarian cancer cell line, is not. Inhibition studies, using GalNAc monosaccharides, are reported here, showing that the labeling is dependent upon the presence of carbohydrate epitopes. The crystal structures of the lectin complexed with two GalNAc containing epitopes associated with cancer, the Tn ({alpha}GalNAc-Ser) and Forssman ({alpha}GalNAc1-3GalNAc) antigens, show the lectin's specificity for GalNAc is due to a particular network of hydrogen bonds. A histidine residue makes hydrophobic contact with the aglycon, rationalizing the preference for GalNAc bearing an additional sugar or amino acid in the a position. These structures provide the molecular basis for the use of HPA in metastasis research.

Key words: Helix pomatia lectin / Tn antigen / Forssman antigen / breast cancer / colon cancer

2 These authors contributed equally to the work.

3 Present address: AFMB-CNRS, 31 Chemin Joseph Aiguier, F-13402, Marseille cedex 20, France


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