Specificity of widely used lectins as probed with oligosaccharide and plant polysaccharide arrays.
Histochem Cell Biol
; 2024 Aug 25.
Article
en En
| MEDLINE
| ID: mdl-39182197
ABSTRACT
Glycan-binding specificity was studied for Jacalin, RCA 120, SBA, PHA-L, PHA-E, WGA, UEA, AAL, LTL, LEL, SNA, DSA, LCA, MAH and Con A, lectins widely used in histochemistry. Oligosaccharide- and polysaccharide-based glycan arrays were applied. Expected specificity was confirmed for only 6 of the 15 lectins and the glycan binding profiles of some lectins were dramatically broader than generally accepted. WGA, LEL and DSA known as chitooligosaccharide-specific, were unexpectedly polyreactive, binding to other glycans with the same affinity as to chitobiose, ABH antigens and oligolactosamines (unsubstituted and sialylated). SBA, in addition to expected binding to glycans with terminal GalNAcα, also had high affinity for the GM1 ganglioside. MAH demonstrated much higher affinity to a variety of sulfated glycans compared to Neu5Acα2-3Galß1-3GalNAcα. Contrary to the common view, LCA demonstrated the maximum binding to (GlcNAcß1-2Manα1)2-3,6-Manß1-4GlcNAcß1-4GlcNAc N-glycan, while it had no interaction with corresponding Gal or Neu5Ac terminated versions. This observed polyreactivity of some lectins casts doubt on their use in accurately determining the presence of a specific glycan structure by histochemical studies. However, comparisons of sera from healthy and diseased individuals with help of a lectin array can easily establish differences in glycosylation patterns and presumptive glycan identities, which can later be clarified using more accurate methods of structural analysis.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Histochem Cell Biol
Asunto de la revista:
CITOLOGIA
/
HISTOCITOQUIMICA
Año:
2024
Tipo del documento:
Article
País de afiliación:
Rusia
Pais de publicación:
Alemania