Abstract

Adenylate cyclase (AC) toxin from B. 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 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 A C 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 of E. coli hemolysin.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.