Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC

Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC

Botulinum neurotoxins (BoNTs) are thought to require complex gangliosides, a group of glycosphingolipids, as essential co-receptors to target neurons. Here, the authors show that BoNT/DC represents an exception to this rule and that an extended loop in BoNT/DC penetrates directly into neuronal membr...

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Main Authors: Sicai Zhang, Ronnie P.-A. Berntsson, William H. Tepp, Liang Tao, Eric A. Johnson, Pål Stenmark, Min Dong
Format: Article
Language:English
Published: Nature Publishing Group 2017-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-01534-z
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spelling doaj-1ace838b4bf145588cda2cd87b10cd112021-05-11T07:42:17ZengNature Publishing GroupNature Communications2041-17232017-11-018111210.1038/s41467-017-01534-zStructural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DCSicai Zhang0Ronnie P.-A. Berntsson1William H. Tepp2Liang Tao3Eric A. Johnson4Pål Stenmark5Min Dong6Department of Urology, Boston Children’s Hospital, Harvard Medical SchoolDepartment of Biochemistry and Biophysics, Stockholm UniversityDepartment of Bacteriology, University of WisconsinDepartment of Urology, Boston Children’s Hospital, Harvard Medical SchoolDepartment of Bacteriology, University of WisconsinDepartment of Biochemistry and Biophysics, Stockholm UniversityDepartment of Urology, Boston Children’s Hospital, Harvard Medical SchoolBotulinum neurotoxins (BoNTs) are thought to require complex gangliosides, a group of glycosphingolipids, as essential co-receptors to target neurons. Here, the authors show that BoNT/DC represents an exception to this rule and that an extended loop in BoNT/DC penetrates directly into neuronal membranes.https://doi.org/10.1038/s41467-017-01534-z
collection DOAJ
language English
format Article
sources DOAJ
author Sicai Zhang
Ronnie P.-A. Berntsson
William H. Tepp
Liang Tao
Eric A. Johnson
Pål Stenmark
Min Dong
spellingShingle Sicai Zhang
Ronnie P.-A. Berntsson
William H. Tepp
Liang Tao
Eric A. Johnson
Pål Stenmark
Min Dong
Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
Nature Communications
author_facet Sicai Zhang
Ronnie P.-A. Berntsson
William H. Tepp
Liang Tao
Eric A. Johnson
Pål Stenmark
Min Dong
author_sort Sicai Zhang
title Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
title_short Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
title_full Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
title_fullStr Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
title_full_unstemmed Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
title_sort structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin dc
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-11-01
description Botulinum neurotoxins (BoNTs) are thought to require complex gangliosides, a group of glycosphingolipids, as essential co-receptors to target neurons. Here, the authors show that BoNT/DC represents an exception to this rule and that an extended loop in BoNT/DC penetrates directly into neuronal membranes.
url https://doi.org/10.1038/s41467-017-01534-z
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AT ronniepaberntsson structuralbasisfortheuniquegangliosideandcellmembranerecognitionmechanismofbotulinumneurotoxindc
AT williamhtepp structuralbasisfortheuniquegangliosideandcellmembranerecognitionmechanismofbotulinumneurotoxindc
AT liangtao structuralbasisfortheuniquegangliosideandcellmembranerecognitionmechanismofbotulinumneurotoxindc
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AT mindong structuralbasisfortheuniquegangliosideandcellmembranerecognitionmechanismofbotulinumneurotoxindc
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