Hemolytic activity of adenylate cyclase toxin from Bordetella pertussis.
FEBS Lett
; 278(1): 79-83, 1991 Jan 14.
Article
em En
| MEDLINE
| ID: mdl-1993477
ABSTRACT
Adenylate cyclase (AC) toxin from B. pertussis enters eukaryotic cells where it produces supraphysiologic levels of cAMP. Purification of AC toxin activity [(1989) J. Biol. Chem. 264, 19279] results in increasing potency of hemolytic activity and electroelution of the 216-kDa holotoxin yields a single protein with AC enzymatic, toxin and hemolytic activities. AC toxin and E. coli hemolysin, which have DNA sequence homology [(1988) EMBO J. 7, 3997] are immunologically cross-reactive. The time courses of hemolysis elicited by the two molecules are strikingly different, however, with AC toxin eliciting cAMP accumulation with rapid onset, but hemolysis with a lag of greater than or equal to 45 min. Finally, osmotic protection experiments indicate that the size of the putative pore produced by AC toxin is 3-5-fold smaller than that of E. coli hemolysin.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bordetella pertussis
/
Fatores de Virulência de Bordetella
/
Proteínas de Escherichia coli
/
Toxina Adenilato Ciclase
/
Proteínas Hemolisinas
/
Hemólise
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1991
Tipo de documento:
Article