posted on 2022-09-20, 19:11authored bySara Bertuzzi, Francesca Peccati, Sonia Serna, Raik Artschwager, Simona Notova, Michel Thépaut, Gonzalo Jiménez-Osés, Franck Fieschi, Niels C. Reichardt, Jesús Jiménez-Barbero, Ana Ardá
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.