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

  1. Madariaga, D. 2
  2. Martínez-Sáez, N. 2
  3. Somovilla, V.J. 2
  4. García-García, Laura. 2
  5. Berbis, M.Á. 1
  6. Valero-Gónzalez, J. 4
  7. Martín-Santamaría, S. 3
  8. Hurtado-Guerrero, R. 4
  9. Asensio, J.L. 5
  10. Jiménez-Barbero, J. 1
  11. Avenoza, A. 2
  12. Busto, J.H. 2
  13. Corzana, F. 2
  14. Peregrina, J.M. 2
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Universidad de La Rioja
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    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  3. 3 Universidad CEU San Pablo
    info

    Universidad CEU San Pablo

    Madrid, España

    ROR https://ror.org/00tvate34

  4. 4 Universidad de Zaragoza
    info

    Universidad de Zaragoza

    Zaragoza, España

    ROR https://ror.org/012a91z28

  5. 5 Instituto de Química Orgánica General
    info

    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

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Journal:
Chemistry - A European Journal

ISSN: 0947-6539

Year of publication: 2014

Volume: 20

Issue: 39

Pages: 12616-12627

Type: Article

DOI: 10.1002/CHEM.201403700 SCOPUS: 2-s2.0-84922568971 WoS: WOS:000342626200036 GOOGLE SCHOLAR lock_openOpen access editor

More publications in: Chemistry - A European Journal

Abstract

The molecular recognition of several glycopeptides bearing Tn antigen (α-O-GalNAc-Ser or α-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