Glycoconjugate Journal

, Volume 35, Issue 2, pp 205–216 | Cite as

Differential recognition of natural and remodeled glycotopes by three Diocleae lectins

  • Tania M. CortázarEmail author
  • Iain B. H. Wilson
  • Alba Hykollari
  • Edgar A. Reyes
  • Nohora A. Vega
Original Article


The carbohydrate specificities of Dioclea grandiflora lectins DGL-I1 and DGL-II, and Galactia lindenii lectin II (GLL-II) were explored by use of remodeled glycoproteins as well as by the lectin hemagglutinating activity against erythrocytes from various species with different glycomic profiles. The three lectins exhibited differences in glycan binding specificity but also showed overlapping recognition of some glycotopes (i.e. Tα glycotope for the three lectins; IIβ glycotope for DGL-II and GLL-II lectins); in many cases the interaction with distinct glycotopes was influenced by the structural context, i.e., by the neighbouring sugar residues. Our data complement and expand the existing knowledge about the binding specificity of these three Diocleae lectins, and taken together with results of previous studies, allow us to suggest a functional map of the carbohydrate recognition which illustrate the impact of modification of basic glycotopes enhancing, permiting, or inhibiting their recognition by each lectin.


Diocleae Dioclea grandiflora Galactia lindenii Lectin specifity Remodeled glycoproteins Hemagglutination 



We thank Dr. R.A. Moreira (University of Fortaleza, Brazil) for his kind gift of D. grandiflora seeds; Dr.J.L. Fernández (Instituto de Ciencias Naturales, Universidad Nacional de Colombia) for species identification and Dr. Wilson’s staff at the Universität für Bodenkultur (BOKU, Vienna, Austria) for training and collaboration. Financial support was provided by the Chemistry Department at the Universidad Nacional - Bogotá, Colombia and COLCIENCIAS with project Lamiaceae Lectin Structure (Grant 110148925106). COLCIENCIAS doctoral student grant (Grant 617 – 0656) facilitated the internship of T.M.Cortázar at the BOKU.

Compliance with ethical standards

Conflicts of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

10719_2018_9812_Fig4_ESM.gif (120 kb)
Figure S1

Enzymatic remodeling of transferrin and fetuin in vitro. The structures of the fetuin native glycans (F5) are based on Refs. [49, 50, 51]. Structures in the remodeled forms of asialoagalactofetuin (F2) and asialofetuin (F3 and F4) result from various combinations of sialidase and galactosidase treatments. F3 was also treated with PNGaseF and, therefore, have no N-glycans. To prepare the transferrin neoglycoforms, the native protein was desialylated and then degalactosylated prior to further modification with recombinant glycosyltransferases as indicate. Symbolic nomenclature is that proposed by the Consortium for Functional Glycomics: circles, hexoses; squares, N-acetylhexosamines; white, galactose stereochemistry; black, glucose stereochemistry; gray, mannose stereochemistry; gray triangle, fucose; black diamond, neuraminic acid. Figures modified from Ref. [16] (GIF 120 kb)

10719_2018_9812_MOESM1_ESM.tif (315 kb)
High Resolution Image (TIFF 314 kb)
10719_2018_9812_MOESM2_ESM.pdf (136 kb)
Supplemental Table S1 (PDF 136 kb)
10719_2018_9812_MOESM3_ESM.pdf (179 kb)
Supplemental Table S2 (PDF 179 kb)
10719_2018_9812_MOESM4_ESM.pdf (139 kb)
Supplemental Table S3 (PDF 139 kb)


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© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • Tania M. Cortázar
    • 1
    Email author
  • Iain B. H. Wilson
    • 2
  • Alba Hykollari
    • 2
  • Edgar A. Reyes
    • 1
  • Nohora A. Vega
    • 1
  1. 1.Protein Research Group, Department of ChemistryUniversidad NacionalBogotáColombia
  2. 2.Molecular Glycobiology Research Group, Department für ChemieUniversität für Bodenkultur (BOKU)WienAustria

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