Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin.
Biochim Biophys Acta
; 1156(2): 213-8, 1993 Feb 13.
Article
em En
| MEDLINE
| ID: mdl-8427878
ABSTRACT
A way of fragmentation of Clostridium botulinum neurotoxin was carried out to elucidate the structure-function relationship of neurotoxin. The hitherto only plausible fragment was isolated from the trypsin-treated heavy chain of botulinum type E neurotoxin. In the presence of 4 M urea, one protein peak emerged from QAE-Sephadex column loaded with the heavy chain mildly treated with trypsin by elution with 0.1 M sodium chloride. Although many protein bands were detected in SDS-PAGE of the treated heavy chain, the eluted protein migrated in a single band to the position of 41,000 Da. The recovery of the 41,000-Da fragment was 28.6%, but with a 2 M urea-containing buffer as eluant, the recovery was less than 12%. The 41,000-Da fragment bound to gangliosides GD1a, GT1b, and GQ1b, to which neurotoxin and the heavy chain bound. The 41,000-Da fragment partially interfered with the binding of 125I-labeled neurotoxin to mouse brain synaptosomes. We have proposed a three-fragment structure (L.H-1.H-2) for botulinum type E neurotoxin. The characters of the 41,000-Da fragment described in this paper seem to substantiated our proposal that type E neurotoxin consists of three fragments, L.H-1.H-2, and that the ganglioside-binding fragment is H-2.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Toxinas Botulínicas
/
Clostridium botulinum
/
Gangliosídeos
Limite:
Animals
Idioma:
En
Ano de publicação:
1993
Tipo de documento:
Article