Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue ACS Central Science Année : 2022

Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin

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 in vitro results to the in vivo environment.

Dates et versions

hal-03917580 , version 1 (02-01-2023)

Identifiants

Citer

Sara Bertuzzi, Francesca Peccati, Sonia Serna, Raik Artschwager, Simona Notova, et al.. Immobilization of Biantennary N-Glycans Leads to Branch Specific Epitope Recognition by LSECtin. ACS Central Science, 2022, 8 (10), pp.1415-1423. ⟨10.1021/acscentsci.2c00719⟩. ⟨hal-03917580⟩
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