Ecto-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exoenzyme S

Infection and Immunity

Volumn 65, Issue 8, 1997, Pages 3304-3309

  Kntght, David A ^a   Barbieri, Joseph T ^a  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A1; BACTERIAL ENZYME; EXOENZYME S; IMMUNOGLOBULIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; UNCLASSIFIED DRUG;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ANIMAL EXPERIMENT; ARTICLE; GRAM NEGATIVE INFECTION; MOLECULAR WEIGHT; NONHUMAN; PLEURA FLUID; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; RABBIT;

EID: 0030858819     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.65.8.3304-3309.1997     Document Type: Article

References (40)

1. Aktories, K., I. Just, and W. Rosenthal. 1988. Different types of ADP-ribose protein bonds formed by botulinum C2 toxin, botulinum ADP-ribosyltransferase C3 and pertussis toxin. Biochem. Biophys. Res. Commun. 156:361-367.
2. Barbieri, J. T., B. K. Moloney, and L. M. Mende-Mueller. 1989. Expression and secretion of the S1 subunit and C180 peptide of pertussis toxin in Escherichia coli. J. Bacteriol. 171:4362-4369.
3. Bjorn, M. J., O. R. Pavlovskis, M. R. Thompson, and B. H. Iglewski. 1979. Production of exoenzyme S during Pseudomonas aeruginosa infections of burned mice. Infect. Immun. 24:837-842.
4. Bodey, G. P., R. Bolivar, V. Fainstein, and L. Jadeja. 1983. Infections caused by Pseudomonas aeruginosa. Rev. Infect. Dis. 5:279-313.
5. Coburn, J. 1992. Pseudomonas aeruginosa exoenzyme S. Curr. Top. Microbiol. Immunol. 175:133-143.
6. Coburn, J., S. T. Dillon, B. H. Iglewski, and D. M. Gill. 1989. Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin. Infect. Immun. 57:996-998.
7. Coburn, J., A. V. Kane, L. Feig, and D. M. Gill. 1991. Pseudomonas aeruginosa exoenzyme S requires a eukaryotic protein for ADP-ribosyltransferase activity. J. Biol. Chem. 266:6438-6446.
8. c-H-ras, are preferred substrates of Pseudomonas aeruginosa exoenzyme S. J. Biol. Chem. 254:9004-9008.
9. Fleiszig, S. M. J., J. P. Wiener-Kronish, H. Miyazaki, V. Vallas, K. E. Mostov, D. Kanada, T. Sawa, T. S. Benedict Yen, and D. W. Frank, 1997. Pseudomonas aeruginosa-mediated cytotoxicity and invasion correlate with distinct genotypes at the loci encoding exoenzyme S. Infect. Immun. 65:579-586.
10. 9a. Frank, D. (Medical College of Wisconsin). Personal communication.
11. Freed, E., M. Symons, S. G. Macdonald, F. McCormick, and R. Ruggieri. 1994. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-1716.
12. Kim, U., M. Kim, J. Kim, M. Han, B. Park, and H. Kim. 1993. Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch. Biochem. Biophys. 305:147-152.
13. Knight, D. A., V. Finck-Barbancon, S. M. Kulich, and J. T. Barbieri. 1995. Functional domains of Pseudomonas aeruginosa exoenzyme S. Infect. Immun. 63:3182-3186.
14. Koch-Nolte, F., F. Haag, R. Kastelein, and F. Bazan. 1996. Uncovered: the family relationship of a T-cell-membrane protein and bacterial toxins. Immunol. Today. 17:30023-30026.
15. Krueger, K. M., and J. T. Barbieri. 1995. The family of bacterial ADP-ribosylating exotoxins. Clin. Microbiol. Rev. 8:34-37.
16. Kudoh, I., J. P. Wiener-Kronish, S. Hashimoto, J. Pittet, and D. Frank. 1994. Exoproduct secretions of Pseudomonas aeruginosa strains influence severity of alveolar epithelial injury. Am. J. Physiol. 267:L551-L556.
17. Kulich, S. M., D. W. Frank, and J. T. Barbieri. 1993. Purification and characterization of exoenzyme S from Pseudomonas aeruginosa 388. Infect. Immun. 61:307-313.
18. Kulich, S. M., T. Yahr, L. Mende-Mueller, J. T. Barbieri, and D. W. Frank. 1994. Cloning the structural gene for the 49 kDa form of exoenzyme S from Pseudomonas aeruginosa strain 388. J. Biol. Chem. 269:10431-10437.
19. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
20. Leffers, H., P. L. Madsen, H. H. Rasmussen, B. Honore, A. H. Andersen, E. Walbum, J. Vanderkerckhove, and J. E. Celis. 1993. Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signaling Pathway. J. Mol. Biol. 231:982-998.
21. Liu, S., T. L. Yahr, D. W. Frank, and J. T. Barbieri. 1997. Biochemical relationships between the 53-kilodalton (Exo53) and 49-kilodalton (ExoS) forms of Exoenzyme S of Pseudomonas aeruginosa. J. Bacteriol. 179:1609-1613.
22. Michiels, R., and G. R. Cornelis. 1991. Secretion of hybrid proteins by the Yersinia Yop export system. J. Bacteriol. 173:1677-1685.
23. Nemoto, E., Y. Yu, and G. Dennert. 1996. Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells. J. Immunol. 157:3341-3349.
24. Ng, W. G., G. N. Donnell, and W. R. Bergren. 1968. Deficiency of erythrocyte nicotinamide adenine dinucleotide nueleosidase (NADase) activity in the Negro. Nature (London) 217:64-65.
25. Nicas, T. I., J. Bradley, J. E. Lochner, and B. H. Iglewski. 1985. The role of exoenzyme S in infections with Pseudomonas aeruginosa. J. Infect. Dis. 152: 716-721.
26. Nicas, T. L, D. W. Frank, P. Stenzel, J. D. Lile, and B. H. Iglewski. 1985. Role of exoenzyme S in chronic Pseudomonas aeruginosa lung infections. Eur. J. Clin. Microbiol. 4:175-179.
27. Nicas, T. I., and B. H. Iglewski. 1984. Isolation and characterization of transposon-induced mutants of Pseudomonas aeruginosa deficient in production of exoenzyme S. Infect. Immun. 45:470-474.
28. Nicas, T. I., and B. H. Iglewski. 1985. Contribution of exoenzyme S to the virulence of Pseudomonas aeruginosa. Antibiot. Chemother. 36:40-48.
29. Nicas, T. L, and B. H. Iglewski. 1985. The contribution of exoproducts to the virulence of Pseudomonas aeruginosa. Can. J. Microbiol. 31:387-392.
30. Olson, J. C., E. M. McGuffie, and D. W. Frank. 1997. Effects of differential expression of the 49-kilodalton exoenzyme S by Pseudomonas aeruginosa on cultured eukaryotic cells. Infect. Immun. 65:248-256.
31. Payne, D. M., E. L. Jacobson, J. Moss, and M. K. Jocobson. 1985. Modification of proteins by mono(ADP-ribosylation) in vivo. Biochemistry 24: 7540-7549.
32. Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
33. Pressler, T., E. T. Jensen, F. Espersen, S. S. Pedersen, and N. Hoiby. 1995. High levels of complement-activation capacity in sera from patients with cystic fibrosis correlate with high levels of IgG3 antibodies to Pseudomonas aeruginosa antigens and poor lung function. Pediatr. Pulmonol. 20:71-77.
34. Reuther, G. W., H. Fu, L. D. Cripe, R. J. Collier, and A. M. Pendergast. 1994. Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family. Science 266:129-133.
35. + :arginine ADP ribosyltransferases with auto-ADP ribosylation activity. J. Immunol. 156:4259-4265.
36. Rosqvist, R., K. Magnusson, and H. Wolf-Watz. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:964-972.
37. Tsuchiya, M., N. Kara, K. Yamada, H. Osdago, and M. Shimoyama. 1994. Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells. J. Biol. Chem. 269:27451-27457.
38. Yahr, T. L., J. T. Barbieri, and D. W. Frank. 1996. Genetic relationship between the 53- and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa. J. Bacteriol. 178:1412-1419.
39. Yahr, T. L., J. Goranson, and D. W. Frank. 1996. Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway. Mol. Microbiol. 22:991-1003.
40. Zolkiewska, A., I. J. Okazaki, and J. Moss. 1994. Vertebrate mono-ADP-ribosyltransferases. Mol. Cell. Biol. 138:107-112.