Interaction of N-linked glycans, having multivalent GlcNAc termini, with GM3 ganglioside |
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Authors: | Seon-Joo Yoon Ken-ichi Nakayama Noriko Takahashi Hirokazu Yagi Natalia Utkina Helen Ying Wang Koichi Kato Martin Sadilek Sen-itiroh Hakomori |
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Institution: | (1) Division of Biomembrane Research, Pacific Northwest Research Institute, and Department of Pathobiology, University of Washington, Seattle, WA, USA;(2) Department of Structural Biology and Biomolecular Engineering, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan;(3) Department of Chemistry, University of Washington, Seattle, WA, USA;(4) Pacific Northwest Research Institute, 720 Broadway, Seattle, WA 98122-4302, USA;(5) Present address: Institute of General Industrial Research, Kagawa, Japan;(6) Present address: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia;(7) Present address: Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, NC, USA |
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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 β-galactosidase, having three or four GlcNAc termini exposed.
These OS, conjugated to phosphatidylethanolamine (PE), showed clear interaction with 3H-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 GalNAcα1-3Gb4 (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.
All solvent ratios are by volume.
An erratum to this article can be found at |
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Keywords: | N-linked oligosaccharide CCI GM3 Multivalent PE conjugate Interaction |
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