Serine versus Threonine Glycosylation with [alpha]-O-GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins

The molecular recognition of several glycopeptides bearing Tn antigen ([alpha]-O-GalNAc-Ser or [alpha]-O-GalNAc-Thr) in their structure by three lectins with affinity for this determinant has been analysed. The work yields remarkable results in terms of epitope recognition, showing that the underlyi...

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Bibliographic Details
Published in:Chemistry : a European journal 2014-09, Vol.20 (39), p.12616
Main Authors: Madariaga, David, Martinez-Saez, Nuria, Somovilla, Víctor J, Garcia-Garcia, Laura, Berbis, M Álvaro, Valero-Gonzalez, Jessika, Martin-Santamaria, Sonsoles, Hurtado-Guerrero, Ramon, Asensio, Juan L, Jimenez-Barbero, Jesús, Avenoza, Alberto, Busto, Jesús H, Corzana, Francisco, Peregrina, Jesús M
Format: Article
Language:English
Subjects:
Antigens
Binding sites
Chemistry
Lectins
Online Access:Get full text
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Summary:The molecular recognition of several glycopeptides bearing Tn antigen ([alpha]-O-GalNAc-Ser or [alpha]-O-GalNAc-Thr) in their structure by three lectins with affinity for this determinant has been analysed. The work yields remarkable results in terms of epitope recognition, showing that the underlying amino acid of Tn (serine or threonine) plays a key role in the molecular recognition. In fact, while Soybean agglutinin and Vicia villosa agglutinin lectins prefer Tn-threonine, Helix pomatia agglutinin shows a higher affinity for the glycopeptides carrying Tn-serine. The different conformational behaviour of the two Tn biological entities, the residues of the studied glycopeptides in the close proximity to the Tn antigen and the topology of the binding site of the lectins are at the origin of these differences. [PUBLICATION ABSTRACT]
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.201403700