Immobilization of Biantennary N‑Glycans Leads to Branch Specific Epitope Recognition by LSECtin
Description
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 Nglycans
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.
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Inmobilization of biantennary N-glycans.pdf
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