Modulation of invasiveness and catalytic activity of Bordetella pertussis adenylate cyclase by polycations.
Penetration of Bordetella pertussis adenylate cyclase into CHO cells was monotonically inhibited by polylysines, with a minimum degree of polymerization of greater than 6 and less than or equal to 9 to 10. Above this level, inhibitory potency per lysyl residue was independent of polymer length; 50% inhibition was obtained with 60 microM lysine monomer. Other polycations were also potent inhibitors. The adenylate cyclase itself showed a biphasic (stimulation-inhibition) response, with a similar independence of polymer length above a certain minimum. Half-maximal inhibitory concentrations for cyclic AMP accumulation corresponded to half-maximal stimulatory concentrations of poly-L-lysine for the cyclase. The inhibitory effect of polylysines on cyclic AMP accumulation was not reversed by washing or enzymatic removal of neuraminic acid. We conclude that charge-charge interactions play an important role in the penetration of B. pertussis adenylate cyclase into host cells.
Raptis
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A
National Institute of Diabetes, Digestive, and Kidney Diseases, Bethesda, Maryland 20892.
Knipling
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LG
Gentile
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Wolff
J
J
D000262:Adenylyl Cyclases / Q000502:physiology*; D000818:Animals; D001886:Bordetella pertussis / Q000187:drug effects / Q000201:enzymology / Q000472:pathogenicity*; D002384:Catalysis; D002460:Cell Line; D005576:Colforsin / Q000494:pharmacology; D006224:Cricetinae; D003412:Cricetulus; D005260:Female; D006657:Histones / Q000494:pharmacology; D008970:Molecular Weight; D010053:Ovary; D011073:Polyamines; D000071228:Polyelectrolytes; D011107:Polylysine / Q000494:pharmacology; D011108:Polymers / Q000494:pharmacology*; D011479:Protamines / Q000494:pharmacology; D014774:Virulence / Q000187:drug effects
D000262:Adenylyl Cyclases; D005576:Colforsin; D006657:Histones; D011073:Polyamines; D000071228:Polyelectrolytes; D011107:Polylysine; D011108:Polymers; D011479:Protamines