ReviewThe FEBS journal2011
Unique ganglioside binding by botulinum neurotoxins C and D-SA.
Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Diagnosis of botulism in mammals aided by toxin ELISA and C and D gene RT-PCRs with an emphasis on farm animals.Veterinary research communications · 2024Article
- Article
- Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy.PLoS biology · 2020Article
- Botulinum and Tetanus Neurotoxins.Annual review of biochemistry · 2019Review
- Host membrane glycosphingolipids and lipid microdomains facilitate Histoplasma capsulatum internalisation by macrophages.Cellular microbiology · 2019Article
- Elucidation of the enigma of glycosphingolipids in the regulation of inflammation and degeneration - Great progress over the last 70 years.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Variations in the Botulinum Neurotoxin Binding Domain and the Potential for Novel Therapeutics.Toxins · 2018Review
- Review
- A lipid-binding loop of botulinum neurotoxin serotypes B, DC and G is an essential feature to confer their exquisite potency.PLoS pathogens · 2018Article
- Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC.Nature communications · 2017Article
- Dissecting the Role of Anti-ganglioside Antibodies in Guillain-Barré Syndrome: an Animal Model Approach.Molecular neurobiology · 2016Review
- Retargeting the Clostridium botulinum C2 toxin to the neuronal cytosol.Scientific reports · 2016Article
- Crystal structures of botulinum neurotoxin DC in complex with its protein receptors synaptotagmin I and II.Structure (London, England : 1993) · 2013Article
- Facing glycosphingolipid-Shiga toxin interaction: dire straits for endothelial cells of the human vasculature.Cellular and molecular life sciences : CMLS · 2013Review
- Unique biological activity of botulinum D/C mosaic neurotoxin in murine species.Infection and immunity · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G), based on a lack of cross-antiserum neutralization. The BoNT/C and BoNT/D serotypes include mosaic toxins that are organized as D-C and C-D toxins. One BoNT D-C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with a vaccine composed of either prototype BoNT/C-Stockholm or BoNT/D-1873. Whereas several BoNT serotypes utilize dual receptors (gangliosides and proteins) to bind to and enter neurons, the basis for BoNT/C and BoNT/D entry into neurons is less well understood. Recent studies solved the crystal structures of the receptor-binding domains of BoNT/C, BoNT/D, and BoNT/D-SA. Comparative structural analysis showed that BoNT/C, BoNT/D and BoNT/D-SA lacked components of the ganglioside-binding pocket that exists within other BoNT serotypes. With the use of structure-based alignments, biochemical analyses, and cell-binding approaches, BoNT/C and BoNT/D-SA have been shown to possess a unique ganglioside-binding domain, the ganglioside-binding loop. Defining how BoNTs enter host cells provides insights towards understanding the evolution and extending the potential therapeutic and immunological values of the BoNT serotypes.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.