Botulinum and Tetanus Neurotoxins

@inproceedings{Niemann1993BotulinumAT,
  title={Botulinum and Tetanus Neurotoxins},
  author={H. Niemann and T. Binz and O. Grebenstein and H. Kurazono and A. Kalkuhl and S. Yamasaki and U. Eisel and J. Pohlner and Germar Schneider and V. Krivan and S. Kozaki and S. Mochida and L. Tauc and B. Poulain},
  booktitle={Springer US},
  year={1993}
}
Dennis L. Leathennan and John L. Middlebrook Department of Immunology and Molecular Biology Toxinology Division United States Anny Medical Research Institute of Infectious Diseases Frederick MD 21702-5011 The phosphorylation of presynaptic proteins was examined in the presence of chlorpromazine using synaptic lysates derived from rat brain synaptosomes that had been preincubated with or without botulinum neurotoxin A. Chlorpromazine increased the phosphorylated state of a number of… Expand
How botulinum and tetanus neurotoxins block neurotransmitter release.
TLDR
How the proteolytic attack at specific sites of the targets for BoNTs and TeNT induces perturbations of the fusogenic SNARE complex dynamics and how these alterations can account for the inhibition of spontaneous and evoked quantal neurotransmitter release by the neurotoxins are explained. Expand
Mechanism of Ganglioside Receptor Recognition by Botulinum Neurotoxin Serotype E
TLDR
The X-ray crystal structure of the binding domain of BoNT/E, a toxin of clinical interest, in complex with its GD1a oligosaccharide receptor is determined and identified key interacting residues that are unique to Bo NT/E and a significant rearrangement of loop 1228–1237 upon carbohydrate binding are identified. Expand
Novel neutralizing human monoclonal antibodies against tetanus neurotoxin
TLDR
Results indicated that antibody clones targeting Hn effectively neutralized TeNT, and the use of a cocktail composed of Hc, Hn, and TeNT mix–reactive antibodies provided enhanced protection compared to theUse of each antibody alone. Expand
Botulinum Toxin Treatment in Surgery, Dentistry, and Veterinary Medicine
Nearly 200 years ago (1820), a young German physician Justinus Kerner predicted that the agent responsible for “sausage poisoning “could have therapeutic implications. The agent Clostridium botulinumExpand
Expression and purification of neurotoxin-associated protein HA-33/A from Clostridium botulinum and evaluation of its antigenicity.
TLDR
A highly expressed and purified recombinant protein is indicated, which is able to evoke high antibody titers in mice, and its antigenicity in mice was studied. Expand
Resolving the Molecular Steps in Clostridial Neurotoxin Light Chain Translocation
TLDR
The current understanding of how CNTs mediate LC translocation is described and the role of the cis-Loop in theLC translocation process relative to other independent functions that have been implicated in LC translocated is placed. Expand
Botulinum versus tetanus neurotoxins: why is botulinum neurotoxin but not tetanus neurotoxin a food poison?
  • B. R. Singh, B. Li, D. Read
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 1995
Botulinum and tetanus neurotoxins, produced by Clostridium botulinum and Clostridium tetani, respectively, are the most poisonous poisons known to mankind. Although botulinum and tetanus neurotoxinsExpand
Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy
TLDR
It is found that HC/DC, C, and G, but not HC/B and HC/D, are capable of binding to receptor-free lipids directly, with HC/ DC having the highest level of binding. Expand
Neurotrophic effects of Botulinum neurotoxin type A in hippocampal neurons involve activation of Rac1 by the non-catalytic heavy chain (HCC/A)
TLDR
It is reported that the non-toxic C-terminal region of the receptor-binding domain of heavy chain BoNT/A (HCC/A) activates the small GTPase Rac1 and ERK pathway to potentiate axonal outgrowth, dendritic protrusion formation and synaptic vesicle release in hippocampal neurons. Expand
Extremely potent Human Monoclonal Antibodies for the Prophylaxis and Therapy of Tetanus
TLDR
It is found that these antibodies interfere with the binding and translocation of the neurotoxin into neurons by interacting with two epitopes, whose definition pinpoints crucial events in the cellular pathogenesis of tetanus. Expand
...
1
2
3
...

References

SHOWING 1-10 OF 142 REFERENCES
Molecular differences between type A botulinum neurotoxin and its toxoid.
TLDR
The physicochemical properties of the toxoid (immunogenic in rabbits) were analyzed and imply that conformational (topographical) antigenic determinants may not contribute significantly to the serological property of the neurotoxin. Expand
Molecular diversity of neurotoxins from Clostridium botulinum type D strains
TLDR
The results indicate that within the type D strains, neurotoxins differ in molecular structure and antigenicity. Expand
Tetanus toxin. The effect of chemical modifications on toxicity, immunogenicity, and conformation.
TLDR
The modification data are consistent with the hypothesis that separate amino acid residues are involved in toxicity and immunogenicity and suggest changes in the local environment of various chromophores. Expand
Study on the immunological heterogeneity of Clostridium botulinum B type toxin.
TLDR
The results suggested immunological heterogeneity of B type botulinum toxin, but for practical purposes, it is not necessary to supplement therapeutic antitoxin with a factor which neutralizes NP toxin. Expand
Toxico-immunologic and serologic relationship of B. botulinus, type C, and B. parabotulinus, “seddon.” XXII.
TLDR
A preliminary study has shown that the C type strains cannot be distinguished morphologically or culturally from the B. parabotulinus strain, and it will be shown in a later paper that the two species are so nearly alike in their metabolism that they cannot be differentiated by the ordinary chemical changes produced in culture mediums. Expand
Basis of Type A and F Toxicities of Clostridium botulinum Strain 84
  • H. Sugiyama, K. Mizutani, K. Yang
  • Chemistry, Medicine
  • Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine
  • 1972
TLDR
Strain 84 culture fluid concentrate, whose toxicity requires for neutralization a mixture of type A and F antitoxins, was absorbed separately with the two types of antitoxin, reducing toxic titer of the type that corresponded to the antitoxin used for absorption to a low level. Expand
Antigenic substructure of tetanus neurotoxin.
  • M. Matsuda, M. Yoneda
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1977
TLDR
Three distinct antigenic determinants were found in the neurotoxin molecule: one in fragment α, released with fragment β by mild trypsin treatment of the toxin, and two in two subfragments (β-1 and β-2) of fragment β. Expand
Botulinum neurotoxin type B (strain 657): partial sequence and similarity with tetanus toxin.
TLDR
The type B neurotoxin isolated from strains 657 and Okra were indistinguishable against polyclonal anti-type B NT serum and the N-terminal amino acid sequences matched exactly with those of the light and heavy chains of type B NT (strain Okra). Expand
Conformational and molecular weight studies of tetanus toxin and its major peptides.
TLDR
Two forms of tetanus toxin have been purified from Clostridium tetani cultures by analytical ultracentrifugation using both conventional and meniscus-depletion sedimentation equilibrium, indicating that the microenvironments of the contributing tryptophans change very little when toxin is dissociated into its constituent chains. Expand
Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity.
TLDR
It is suggested that the primary site(s) of tryptic action on the heavy subunit of botulinum type A neurotoxin is close to the COOH terminus and that cleavage of the polypeptide chain in this region results in a loss of toxic activity mediated by the destruction of the neurotoxin-binding site. Expand
...
1
2
3
4
5
...