Adenylate Bordetella pertussis

Ladant, D., Glaser, P., and Ullmann, A. (1992). Insertional mutagenesis of Bordetella pertussis adenylate cyclase./. Biol. Chem., 267, 2244-2250. 

Friedman, R.L., Fiederlein, R.L., Glasser, L., Galgiani, J.N. (1987). Bordetella pertussis adenylate cyclase effects of affinity-purified adenylate cyclase on human polymorphonuclear leukocyte functions. Infect. Immun. 55 135 0. 

Hackett M, Guo L, Shabanowitz J et al. (1994) Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis. In Science 266 433-435. 

Donovan MG, Storm DR (1990) Evidence that the adenylate cyclase secreted from Bordetella pertussis does not enter animal cells by receptor-mediated endocyto-sis. J Cell Physiol 145 444-449. 

Hanski H, Farfel Z (1985) Bordetella pertussis invasive adenylate cyclase. J Biol Chem 260 5526-5532. 

The secretory product of Bordetella pertussis interferes with the ability of agonists to inhibit adenylate cyclase. It catalyzes the transfer of the ADP-ribose moiety of NAD+ to a cysteine residue close to the carboxy terminus of Gi,. 

The synthesis of the two diastereoisomers of P -l-(2-nitrophenyl)ethyl adenosine S -lri-phosphate (91) has been achieved using resolved (R)- and (5)-l-(2-nilroidienyl)ethanol. The alcohols were converted to (R)- and (5)-l-(2-nitrophenyl)ethyl phosphates by phosphitylation with N,)V-diisopropyl-fi(s-(2-cyanoethyl)phosphoramidite (92) and subsequent oxidation with 3-chlorobenzoic acid. Each of the monophosphates was activated with carbonyidiimidazole and condensed with adenosine diphosphate to give the desired triphosphate. These ATP analogues can be used for the rapid release (by flash photolysis) of ATP in biological systems. The 8-azido-3 -0-anthraniloyl derivatives of 2 -dADP (93) and 2 -dATP (94) have been prepared in seven steps from 8-azido-2 -deoxyadenosine. These compounds are of interest as fluorescent and photoactivatable probes for the nucleotide binding site of kinases and cyclases. In particular, (94) was shown to be a competitive inhibitor of Bordetella pertussis adenylate cyclase and the observed K- (74 pM) was close to tiiat predicted from the K- value of 3 -0-anthraniloyl-2 -dATP. ... 

Guermonprez P, Khelef N, Blouin et al. The adenylate cyclase toxin of bordetella pertussis binds to target cells via the alpha(M)beta(2) integrin (CDllb/CD18). J Exp Med 2001 193(9) 1035-1044. 

Goodwin MS, Weiss AA. Adenylate cyclase toxin is critical hr colonization and pertussis toxin is critical for lethal infection by Bordetella pertussis in infant mice. Infect Immun 1990 58(10) 3445-3447. 

Carbonetti NH, Artamonova GV, Andreasen C et al. Pertussis toxin and adenylate cyclase toxin provide a one-two punch for establishment of bordetella pertussis infection of the respiratory tract. Infect Immun 2005 73(5) 2698-2703. 

Ort B, Douce G, Baillie S et al. Adjuvant eftftets of adenylate cyclase toxin of bordetella pertussis after intranasal immunisation of mice. Vaccine 2007 25(1) 64-71. 

Ross PJ, Lavelle EC, Mills KH et al. Adenylate cyclase toxin from bordetella pertussis synergizes with lipopolysaccharide to promote innate interleukin-10 production and enhances the induction of 7h2 and regulatory T-cells. Infect Immun 2004 72(3) 1568-1579. 

Dadaglio G, Moukrim Z, Lo-Man R et aL Induction of a polarized Ihl response by insertion of multiple copies of a viral T-cell epitope into adenylate cyclase of bordetella pertussis. Infect immun 2000 68(7) 3867-3872. 

Khelef N, Zychlinsky A, Guiso N. Bordetella pertussis induces apoptosis in macrophages role of adenylate cyclase-hemolysin. Infect Immun 1993 61(10) 4064-4071. 

Gueirard P, Druilhe A, Pretolani M et al. Role of adenylate cyclase-hemolysin in alveolar macrophage apoptosis during bordetella pertussis infection in vivo. Infect Immun 1998 66(4) 1718-1725. 

Boyd AP, Ross PJ, Conroy H et al. Bordetella pertussis adenylate cyclase toxin modulates innate and adaptive immune responses distinct roles for acylation and enzymatic activity in immunomodulation and cell death. J Immunol 2005 175(2) 730-738. 

Pearson RD, Symes P, Conboy M et al. Inhibition of monocyte oxidative responses by bordetella pertussis adenylate cyclase toxin. J Immunol 1987 139(8) 2749-27. ... 

Njamkepo E, Pinot F, Francois D et al. Adaptive responses of human monocytes infected by bordetella pertussis the role of adenylate cyclase hemolysin. J Cell Physiol 2000 183(l) 91-99. 

Spensieri F, Fedele G, Fazio C et al. Bordetella pertussis inhibition of interleukin-12 (IL-12) p70 in human monocyte-derived dendritic cells blocks IL-12 p35 through adenylate cyclase toxin-dependent cyclic AMP induction. Infect Immun 2006 74(5) 2831-2838. 

Fayolle C, Sebo P, Ladant D et al. In vivo induction of CTL responses by recombinant adenylate cyclase of Bordetella pertussis carrying viral CD8+ T-cell epitopes. J Immunol 1996 156(12) 4697-4706. 

Saron MF, Fayolle C, Sebo P et al. Anti-viral protection conferred by recombinant adenylate cyclase toxins from bordetella pertussis carrying a CD8+ T-cell epitope from lymphocytic choriomeningitis virus. Proc Natl Acad Sci USA 1997 94(7) 3314-3319. 

Fayolle C, Ladant D, Karimova G et al. Therapy of murine tumors with recombinant bordetella pertussis adenylate cyclase carrying a cytotoxic T-cell epitope. J Immunol 1999 162(7) 4157-4162. 

Fayolle C, Osickova A, Osicka R et al. Delivery of multiple epitopes by recombinant detoxified adenylate cyclase of bordetella pertussis induces protective antiviral immunity. J Virol 2001 75(16) 7330-7338. 

Loucka J, Schlecht G, Vodolanova J et al. Delivery of a MalE CD4(+)-T-cell epitope into the major histocompatibility complex class II antigen presentation pathway by bordetella pertussis adenylate cyclase. Infect Immun 2002 70(2) 1002-1005. 

Adenylate cyclase (EC 4.6.1.1). Abundant information is available on the properties and distribution of this enzyme and it need not be recited here. Characteristically, this enzyme is associated with the cytoplasmic aspect of the plasma membrane (TRAMS LAUTER, 1974 CUTLER, 1974). It, therefore, should serve as an excellent marker for preparations in which the integrity of right-side-out or inside-out vesicles has to be assayed. Adenylate cyclase, also, is one of the membrane enzymes for which a physiological role is clearly established. The localization of this enzyme on the inside of the plasma membrane makes good biological sense. We advocated the use of adenylate cyclase as a marker for the inside of the plasma membrane but must emphasize that the enzyme is not necessarily confined to that aspect of the membrane in all species. In Bordetella pertussis an extracyto-plasmic adenylate cyclase enables intact organisms to form cAMP from exogenous ATP (HEWLETT et al., 1976). 

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