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Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside. | LitMetric

Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside.

Glycoconj J

Division of Biomembrane Research, Pacific Northwest Research Institute, and Department of Pathobiology, University of Washington, Seattle, WA, USA.

Published: December 2006

AI Article Synopsis

  • - GM3 ganglioside specifically interacts with complex-type N-linked glycans that have multiple GlcNAc termini, showing clear binding with certain oligosaccharides from ovalbumin and fetuin.
  • - The study identifies previously unreported N-linked glycan structures and emphasizes that GM3 had a stronger interaction with certain glycan-PE conjugates compared to others.
  • - These findings suggest that the interactions between specific N-linked glycans and GM3 ganglioside may play a significant role in cell biology, warranting further investigation into their natural occurrences.

Article Abstract

GM3 ganglioside interacts specifically with complex-type N-linked glycans having multivalent GlcNAc termini, as shown for (1) and (2) below. (1) Oligosaccharides (OS) isolated from ConA-non-binding N-linked glycans of ovalbumin, whose structures were identified as penta-antennary complex-type with bisecting GlcNAc, having five or six GlcNAc termini (OS B1, B2), or bi-antennary complex-type having two GlcNAc termini (OS I). OS I is a structure not previously described. (2) Multi-antennary complex-type N-linked OS isolated from fetuin, treated by sialidase followed by beta-galactosidase, having three or four GlcNAc termini exposed. These OS, conjugated to phosphatidylethanolamine (PE), showed clear interaction with (3)H-labeled liposomes containing GM3, when various doses of OS-PE conjugate were adhered by drying to multi-well polystyrene plates. Interaction was clearly observed only with liposomes containing GM3, but not LacCer, Gb4, or GalNAcalpha1-3Gb4 (Forssman antigen). GM3 interaction with PE conjugate of OS B1 or B2 was stronger than that with PE conjugate of OS I. GM3 interacted clearly with PE conjugate of N-linked OS from desialylated and degalactosylated fetuin, but not native fetuin. No binding was observed to cellobiose-PE conjugate, or to OS-PE conjugate lacking GlcNAc terminus. Thus, GM3, but not other GSL liposomes, interacts with various N-linked OS having multiple GlcNAc termini, in general. These findings suggest that the concept of carbohydrate-to-carbohydrate interaction can be extended to interaction of specific types of N-linked glycans with specific GSLs. Natural occurrence of such interaction to define cell biological phenomena is under investigation.

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Source
http://dx.doi.org/10.1007/s10719-006-9001-4DOI Listing

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