NDLI: Gangliosides as high affinity receptors for tetanus neurotoxin.

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Gangliosides as high affinity receptors for tetanus neurotoxin.

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Gangliosides as high affinity receptors for tetanus neurotoxin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kim, Jung-ja P. Fu, Zhuji Barbieri, Joseph T. Chen, Chen Baldwin, Michael R.
Description	Author Affiliation: Chen C ( Department of Microbiology and Molecular Genetics, Medical College of Wisconsin,Milwaukee, Wisconsin 53226, USA.)
Abstract	Tetanus neurotoxin (TeNT) is an exotoxin produced by Clostridium tetani that causes paralytic death to hundreds of thousands of humans annually. TeNT cleaves vesicle-associated membrane protein-2, which inhibits neurotransmitter release in the central nervous system to elicit spastic paralysis, but the molecular basis for TeNT entry into neurons remains unclear. TeNT is a approximately 150-kDa protein that has AB structure-function properties; the A domain is a zinc metalloprotease, and the B domain encodes a translocation domain and C-terminal receptor-binding domain (HCR/T). Earlier studies showed that HCR/T bound gangliosides via two carbohydrate-binding sites, termed the lactose-binding site (the 'W' pocket) and the sialic acid-binding site (the 'R' pocket). Here we report that TeNT high affinity binding to neurons is mediated solely by gangliosides. Glycan array and solid phase binding analyses identified gangliosides that bound exclusively to either the W pocket or the R pocket of TeNT; GM1a bound to the W pocket, and GD3 bound to the R pocket. Using these gangliosides and mutated forms of HCR/T that lacked one or both carbohydrate-binding pocket, gangliosides binding to both of the W and R pockets were shown to be necessary for high affinity binding to neuronal and non-neuronal cells. The crystal structure of a ternary complex of HCR/T with sugar components of two gangliosides bound to the W and R supported the binding of gangliosides to both carbohydrate pockets. These data show that gangliosides are functional dual receptors for TeNT.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	39
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-09-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Clostridium Tetani Metabolism Gangliosides Metalloendopeptidases Tetanus Toxin Animals Binding Sites Genetics Binding, Competitive Cell Line, Tumor Cerebral Cortex Cytology Crystallization Crystallography, X-Ray Endopeptidase K Chemistry HeLa Cells Hydrolysis Kinetics Mutation Neurons PC12 Cells Polysaccharides Protein Binding Vesicle-Associated Membrane Protein 2 Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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