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Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin
[Image: see text] 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 epito...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9615123/ https://www.ncbi.nlm.nih.gov/pubmed/36313162 http://dx.doi.org/10.1021/acscentsci.2c00719 |
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author | Bertuzzi, Sara Peccati, Francesca Serna, Sonia Artschwager, Raik Notova, Simona Thépaut, Michel Jiménez-Osés, Gonzalo Fieschi, Franck Reichardt, Niels C. Jiménez-Barbero, Jesús Ardá, Ana |
author_facet | Bertuzzi, Sara Peccati, Francesca Serna, Sonia Artschwager, Raik Notova, Simona Thépaut, Michel Jiménez-Osés, Gonzalo Fieschi, Franck Reichardt, Niels C. Jiménez-Barbero, Jesús Ardá, Ana |
author_sort | Bertuzzi, Sara |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-9615123 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-96151232022-10-29 Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin Bertuzzi, Sara Peccati, Francesca Serna, Sonia Artschwager, Raik Notova, Simona Thépaut, Michel Jiménez-Osés, Gonzalo Fieschi, Franck Reichardt, Niels C. Jiménez-Barbero, Jesús Ardá, Ana ACS Cent Sci [Image: see text] 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. American Chemical Society 2022-09-20 2022-10-26 /pmc/articles/PMC9615123/ /pubmed/36313162 http://dx.doi.org/10.1021/acscentsci.2c00719 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Bertuzzi, Sara Peccati, Francesca Serna, Sonia Artschwager, Raik Notova, Simona Thépaut, Michel Jiménez-Osés, Gonzalo Fieschi, Franck Reichardt, Niels C. Jiménez-Barbero, Jesús Ardá, Ana Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin |
title | Immobilization of Biantennary N-Glycans Leads
to Branch Specific Epitope Recognition by LSECtin |
title_full | Immobilization of Biantennary N-Glycans Leads
to Branch Specific Epitope Recognition by LSECtin |
title_fullStr | Immobilization of Biantennary N-Glycans Leads
to Branch Specific Epitope Recognition by LSECtin |
title_full_unstemmed | Immobilization of Biantennary N-Glycans Leads
to Branch Specific Epitope Recognition by LSECtin |
title_short | Immobilization of Biantennary N-Glycans Leads
to Branch Specific Epitope Recognition by LSECtin |
title_sort | immobilization of biantennary n-glycans leads
to branch specific epitope recognition by lsectin |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9615123/ https://www.ncbi.nlm.nih.gov/pubmed/36313162 http://dx.doi.org/10.1021/acscentsci.2c00719 |
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