Production, purification and characterization of Clostridium difficile toxic proteins different from toxin A and from toxin B.
Biochim Biophys Acta
; 998(2): 151-7, 1989 Oct 05.
Article
em En
| MEDLINE
| ID: mdl-2506935
ABSTRACT
The purification and characterization of three new proteins called C1, C2, and C3 from Clostridium difficile are described. Their estimated molecular mass were about 350 (C1), 270 (C2) and 140 (C3) kDa, consisting of subunits of 39 (C1), 43 (C2) and 41 (C3) kDa, respectively. Immunodiffusion revealed that the three proteins contained similar but not identical antigenic determinants to toxin A. Each protein induced a cytotonic effect on hamster ovaric cells; the combined proteins, had a specific activity on cells 5-times higher than that of toxin A. In rat intestinal loops, they induced a clear fluid secretion, while toxin A elicited a haemorrhagic fluid response. The cytotonic activities of all three proteins were abolished by antiserum against toxin A, while antiserum against toxin B inhibited only the activity of the 270 kDa protein. In contrast to toxin A, the cytotoxicity of the three proteins was inactivated by trypsin. Thus, the chemical, antigenic and biological properties of these proteins differed from those of toxin A and toxin B.
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Base de dados:
MEDLINE
Assunto principal:
Toxinas Bacterianas
/
Clostridium
Idioma:
En
Ano de publicação:
1989
Tipo de documento:
Article