Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin.
Journal
ACS central science
ISSN: 2374-7943
Titre abrégé: ACS Cent Sci
Pays: United States
ID NLM: 101660035
Informations de publication
Date de publication:
26 Oct 2022
26 Oct 2022
Historique:
received:
20
06
2022
entrez:
31
10
2022
pubmed:
1
11
2022
medline:
1
11
2022
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 36313162
doi: 10.1021/acscentsci.2c00719
pmc: PMC9615123
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1415-1423Subventions
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Informations de copyright
© 2022 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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