Lipid interaction of Tetanus neurotoxin A calorimetric and fluorescence spectroscopy study

Calappi, E.; Masserini, Massimo; Schiavo, Giampietro; Montecucco, Cesare; Tettamanti, Guido

doi:10.1016/0014-5793(92)81074-v

Cited by 16 publications

(9 citation statements)

References 25 publications

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“…As the Tet C fragment is the membrane-binding domain, it is likely that its interactions with G T1b would be sensitive to changes in pH. This result is in contrast to work by others who have examined the formation of pores in lipid membranes by the full-length tetanus toxin at low pH (57)(58)(59)(60).…”

Section: Figurementioning

confidence: 79%

In Situ Scanning Probe Microscopy Studies of Tetanus Toxin-Membrane Interactions

Slade

Schoeniger

Sasaki

et al. 2006

Biophysical Journal

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Despite the considerable information available with regards to the structure of the clostridial neurotoxins, and their inherent threat as biological warfare agents, the mechanisms underpinning their interactions with and translocation through the cell membrane remain poorly understood. We report herein the results of an in situ scanning probe microscopy study of the interaction of tetanus toxin C-fragment (Tet C) with supported planar lipid bilayers containing the ganglioside receptor G(T1b). Our results show that Tet C preferentially binds to the surface of fluid phase domains within biphasic membranes containing G(T1b) and that with an extended incubation period these interactions lead to dramatic changes in the morphology of the lipid bilayer, including the formation of 40-80 nm diameter circular cavities. Combined atomic force microscopy/total internal reflection fluorescence microscopy experiments confirmed the presence of Tet C in the membrane after extended incubation. These morphological changes were found to be dependent upon the presence of G(T1b) and the solution pH.

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Section: Figurementioning

confidence: 79%

In Situ Scanning Probe Microscopy Studies of Tetanus Toxin-Membrane Interactions

Slade

Schoeniger

Sasaki

et al. 2006

Biophysical Journal

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“…Ean der Goot, Gonzalez-Manas, Lakey, and Pattus (1991) observed that, depending on circumstances, the pH in the vicinity of the membrane might be 1-3 units lower than in the bulk solution. A decrease in pH has been linked to structural changes in many proteins, such as the Bt toxin Cry1C (Butko, Cournoyer, Pusztai-Carey, & Surewicz, 1994), P. aeruginosa exotoxin A (Menestrina, Pederzolli, Forti, & Gambale, 1991), tetanus toxin (Calappi, Masserini, Schiavo, Montecucco, & Tettamanti, 1992), and tumor necrosis factor a (Kagan, Baldwin, Munoz, & Wisnieski, 1992). All of these proteins increase their affinity to the membrane at acidic pH (Manceva, Pusztai-Carey, & Butko, 2004).…”

Section: Antimicrobial Activity and Hemolytic Activitymentioning

confidence: 97%

Discovery of a novel antimicrobial peptide using membrane binding-based approach

et al. 2009

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“…There is experimental evidence that glycolipid‐enriched domains are a target for certain diseases, some of them of particular interest for the nervous system: Alzheimer’s disease, prion diseases, and neurolipidoses, which will be discussed. However, it is worth reminding that also the neuron‐specific toxin of Clostridium tetani induces, in vitro, formation of ganglioside domains, which were postulated to be involved in the mechanism of toxin internalization (Calappi et al, 1992).…”

Section: Pathological Implicationsmentioning

confidence: 99%

Glycolipid‐Enriched Caveolae and Caveolae‐Like Domains in the Nervous System

Masserini

Palestini

Pitto

1999

Journal of Neurochemistry

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104

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Recent years have been characterized by a booming interest in research on caveolae and caveolaelike membrane domains. The interest in this subject grew further, when their involvement in fundamental membrane-associated events, such as signal transmission and lipid/protein sorting, was postulated. Substantial progress has been reached in understanding the biological role of membrane domains in eukaryotic cells. The neuron, however, which perhaps represents one of the greatest challenges to research on membrane traffic and function, has only been partially investigated. The purpose of the present review is to survey this issue in the nervous system. We confine ourselves to the presence of membrane domains in the nervous system and discuss this in the context of three facts: first, glycolipids are peculiarly enriched in both caveolae and caveolae-like domains and are particularly abundant in the nervous system; second, the neuron is characterized by a basic dual polarity, similar in this respect to other polarized cells, where the role of glycolipid-enriched domains for lipid/protein sorting has been better ascertained; and third, neurons evolved from, and are related to, simpler eukaryotic cells, allowing us to find analogies with more investigated nonneuronal cells.

show abstract

Lipid interaction of Tetanus neurotoxin A calorimetric and fluorescence spectroscopy study

Cited by 16 publications

References 25 publications

In Situ Scanning Probe Microscopy Studies of Tetanus Toxin-Membrane Interactions

In Situ Scanning Probe Microscopy Studies of Tetanus Toxin-Membrane Interactions

Discovery of a novel antimicrobial peptide using membrane binding-based approach

Glycolipid‐Enriched Caveolae and Caveolae‐Like Domains in the Nervous System

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