Immobilization of biantennary N-glycans leads to branch specific epitope recognition by LSECtin Journal Article


Authors: Bertuzzi, S.; Peccati, F.; Serna, S.; Artschwager, R.; Notova, S.; Thépaut, M.; Jiménez-Osés, G.; Fieschi, F.; Reichardt, N. C.; Jiménez-Barbero, J.; Ardá, A.
Article Title: Immobilization of biantennary N-glycans leads to branch specific epitope recognition by LSECtin
Abstract: The molecular recognition features of LSECtin toward asymmetric N-glycans have been scrutinized by NMR and compared to those occurring in glycan microarrays. A pair of positional glycan isomers (LDN3 and LDN6), a nonelongated GlcNAc4Man3 N-glycan (G0), and the minimum binding epitope (the GlcNAcβ1-2Man disaccharide) have been used to shed light on the preferred binding modes under both experimental conditions. Strikingly, both asymmetric LDN3 and LDN6 N-glycans are recognized by LSECtin with similar affinities in solution, in sharp contrast to the results obtained when those glycans are presented on microarrays, where only LDN6 was efficiently recognized by the lectin. Thus, different results can be obtained using different experimental approaches, pointing out the tremendous difficulty of translating in vitro results to the in vivo environment. © 2022 American Chemical Society. All rights reserved.
Keywords: binding energy; polysaccharides; glycans; experimental conditions; epitopes; isomers; n-glycan; immobilisation; binding epitopes; binding modes; experimental approaches; glycan microarrays; recognition features; sharp contrast
Journal Title: ACS Central Science
Volume: 8
Issue: 10
ISSN: 2374-7943
Publisher: American Chemical Society  
Date Published: 2022-10-26
Start Page: 1415
End Page: 1423
Language: English
DOI: 10.1021/acscentsci.2c00719
PROVIDER: scopus
PMCID: PMC9615123
PUBMED: 36313162
DOI/URL:
Notes: Article -- Export Date: 1 December 2022 -- Source: Scopus
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