Hemolytic activity of adenylate cyclase toxin fromBordetella pertussis

Abstract

Adenylate cyclase (AC) toxin fromB. pertussis enters eukaryotic cells where it produces supraphysiologie 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 andE. 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 ≥ 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 ofE. coli hemolysin.