Specificity of viscumin revised. As probed with a printed glycan array.
Printed glycan array
Sialoglycan
Sulfated glycan
Viscumin
αGal epitope
Journal
Biochimie
ISSN: 1638-6183
Titre abrégé: Biochimie
Pays: France
ID NLM: 1264604
Informations de publication
Date de publication:
Nov 2022
Nov 2022
Historique:
received:
06
07
2022
revised:
11
08
2022
accepted:
13
08
2022
pubmed:
22
8
2022
medline:
23
11
2022
entrez:
21
8
2022
Statut:
ppublish
Résumé
Viscumin, a lectin used in anti-cancer therapy, was originally considered as βGal recognizing protein; later, an ability to bind 6'-sialyl N-acetyllactosamine (6'SLN) terminated gangliosides was found. Here we probed viscumin with a printed glycan array (PGA) containing a large number of mammalian sulfated glycans, and found a strong binding to glycans with 6-O-SuGal moiety as lactose, N-acetyllactosamine (LN), di-N-acetyllactosamine (LacdiNAc), and even 6-O-SuGalNAcα (but not SiaTn). Also, the ability to bind some of αGal terminated glycans, including Galα1-3Galβ1-4GlcNAc, was observed. Unexpectedly, only weak interaction was detected with parent neutral β-galactosides including LN-LN-LN and branched (LN)
Identifiants
pubmed: 35988841
pii: S0300-9084(22)00213-9
doi: 10.1016/j.biochi.2022.08.009
pii:
doi:
Substances chimiques
Lactose
J2B2A4N98G
mistletoe lectin I
0
Polysaccharides
0
Ribosome Inactivating Proteins, Type 2
0
Sulfates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
94-102Informations de copyright
Copyright © 2022 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.