Temperature‐Mediated Interaction of Tetanus Toxin with Cerebral Neuron Cultures: Characterization of a Neuraminidase‐Insensitive Toxin‐Receptor Complex

Temperature‐Mediated Interaction of Tetanus Toxin with Cerebral Neuron Cultures:... Abstract: Energy‐dependent internalization of 125I‐labeled tetanus toxin into cultured neural cells is shown to follow an energy‐independent binding process. A three‐step model, involving receptor‐mediated binding followed by sequestration and internalization is proposed. In the first step, binding of toxin is enhanced in appearance under low ionic strength medium, at 0–4°C; it is suppressed, however, with increasing incubation temperature under physiological salt concentrations. Cell‐bound toxin is displaced by approximately 35.5% when high‐salt medium (physiological concentrations) is added to cells at 0–4°C; the effect is further amplified at 37°C. Addition of disialoganglioside GD1b (1–5 μg/ml) also lowers the amount of cell‐associated toxin. The fraction of 125I‐labeled toxin retained by the cells after exposure to high‐salt medium at 0–4°C or after addition of GD1b is operationally defined as sequestered toxin. This second step, characterized by a stable association of the toxin with the neural cells, is affected by both physiological salt and by 37°C conditions. Lastly, an energy‐dependent phenomenon of firm association of tetanus toxin with neural cells, compatible with internalization, is described. The toxin residing in this fraction is bioactive and cannot be removed by salts, gangliosides, or by treatment with protease or neuraminidase. Binding, sequestration, and internalization are mutually dependent, as they are all blocked by pretreatment of cells with neuraminidase and by an enhanced energy‐independent sequestration event, which results in enhanced tetanus toxin internalization by an energy‐dependent process. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

Temperature‐Mediated Interaction of Tetanus Toxin with Cerebral Neuron Cultures: Characterization of a Neuraminidase‐Insensitive Toxin‐Receptor Complex

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Publisher
Wiley
Copyright
1983 International Society for Neurochemistry
ISSN
0022-3042
eISSN
1471-4159
DOI
10.1111/j.1471-4159.1983.tb13559.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: Energy‐dependent internalization of 125I‐labeled tetanus toxin into cultured neural cells is shown to follow an energy‐independent binding process. A three‐step model, involving receptor‐mediated binding followed by sequestration and internalization is proposed. In the first step, binding of toxin is enhanced in appearance under low ionic strength medium, at 0–4°C; it is suppressed, however, with increasing incubation temperature under physiological salt concentrations. Cell‐bound toxin is displaced by approximately 35.5% when high‐salt medium (physiological concentrations) is added to cells at 0–4°C; the effect is further amplified at 37°C. Addition of disialoganglioside GD1b (1–5 μg/ml) also lowers the amount of cell‐associated toxin. The fraction of 125I‐labeled toxin retained by the cells after exposure to high‐salt medium at 0–4°C or after addition of GD1b is operationally defined as sequestered toxin. This second step, characterized by a stable association of the toxin with the neural cells, is affected by both physiological salt and by 37°C conditions. Lastly, an energy‐dependent phenomenon of firm association of tetanus toxin with neural cells, compatible with internalization, is described. The toxin residing in this fraction is bioactive and cannot be removed by salts, gangliosides, or by treatment with protease or neuraminidase. Binding, sequestration, and internalization are mutually dependent, as they are all blocked by pretreatment of cells with neuraminidase and by an enhanced energy‐independent sequestration event, which results in enhanced tetanus toxin internalization by an energy‐dependent process.

Journal

Journal of NeurochemistryWiley

Published: May 1, 1983

References

  • Binding characteristics of 125 I‐labeled tetanus toxin to primary tissue cultures from mouse embryonic CNS
    Dimpfel, Dimpfel; Habermann, Habermann
  • Sequestration of tetanus toxin in developing neuronal cell cultures
    Yavin, Yavin; Yavin, Yavin; Kohn, Kohn

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