메뉴 건너뛰기




Volumn 77, Issue 10, 2009, Pages 4362-4370

Characterization of a unique ADP-ribosyltransferase of Mycoplasma penetrans

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMMONIUM CHLORIDE; BACTERIAL PROTEIN; CELL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; PERTUSSIS TOXIN; PROTEIN MYPE9110; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 70349436041     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00044-09     Document Type: Article
Times cited : (11)

References (38)
  • 4
    • 0031731387 scopus 로고    scopus 로고
    • Protein kinase C activation and vacuolation in HeLa cells invaded by Mycoplasma penetrans
    • Borovsky, Z., M. Tarshis, P. Zhang, and S. Rottem. 1998. Protein kinase C activation and vacuolation in HeLa cells invaded by Mycoplasma penetrans. J. Med. Microbiol. 47:915-922.
    • (1998) J. Med. Microbiol. , vol.47 , pp. 915-922
    • Borovsky, Z.1    Tarshis, M.2    Zhang, P.3    Rottem, S.4
  • 5
    • 0024280875 scopus 로고
    • Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope
    • Burnette, W. N., W. Cieplak, V. L. Mar, K. T. Kaljot, H. Sato, and J. M. Keith. 1988. Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope. Science 242:72-74.
    • (1988) Science , vol.242 , pp. 72-74
    • Burnette, W.N.1    Cieplak, W.2    Mar, V.L.3    Kaljot, K.T.4    Sato, H.5    Keith, J.M.6
  • 6
    • 0021280847 scopus 로고
    • NAD binding site of diphtheria toxin: Identification of a residue within the nicotinamide subsite by photochemical modification with NAD
    • Carroll, S. F., and R. J. Collier. 1984. NAD binding site of diphtheria toxin: identification of a residue within the nicotinamide subsite by photochemical modification with NAD. Proc. Natl. Acad. Sci. USA 81:3307-3311.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3307-3311
    • Carroll, S.F.1    Collier, R.J.2
  • 7
    • 0023790330 scopus 로고
    • Identification of a region in the S1 subunit of pertussis toxin that is required for enzymatic activity and that contributes to the formation of a neutralizing antigenic determinant
    • Cieplak, W., W. N. Burnette, V. L. Mar, K. T. Kaljot, C. F. Morris, K. K. Chen, H. Sato, and J. M. Keith. 1988. Identification of a region in the S1 subunit of pertussis toxin that is required for enzymatic activity and that contributes to the formation of a neutralizing antigenic determinant. Proc. Natl. Acad. Sci. USA 85:4667-4671.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4667-4671
    • Cieplak, W.1    Burnette, W.N.2    Mar, V.L.3    Kaljot, K.T.4    Morris, C.F.5    Chen, K.K.6    Sato, H.7    Keith, J.M.8
  • 9
    • 0026713040 scopus 로고
    • Potentiation of Helicobacter pylori vacuolating toxin activity by nicotine and other weak bases
    • Cover, T. L., S. G. Vaughn, P. Cao, and M. J. Blaser. 1992. Potentiation of Helicobacter pylori vacuolating toxin activity by nicotine and other weak bases. J. Infect. Dis. 166:1073-1078.
    • (1992) J. Infect. Dis. , vol.166 , pp. 1073-1078
    • Cover, T.L.1    Vaughn, S.G.2    Cao, P.3    Blaser, M.J.4
  • 10
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., E. Wallin, I. Simon, G. von Heijne, and A. Elofsson. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10:673-676. (Pubitemid 27332074)
    • (1997) Protein Engineering , vol.10 , Issue.6 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 11
    • 0033679277 scopus 로고    scopus 로고
    • Intracellular DNA replication and long-term survival of pathogenic mycoplasmas
    • Dallo, S. F., and J. B. Baseman. 2000. Intracellular DNA replication and long-term survival of pathogenic mycoplasmas. Microb. Pathog. 29:301-309.
    • (2000) Microb. Pathog. , vol.29 , pp. 301-309
    • Dallo, S.F.1    Baseman, J.B.2
  • 12
    • 0002090806 scopus 로고
    • Bacterial ADP-ribosyltransferases
    • J. Moss, B. Iglewski, M. Vaughan, and A. Tu (ed.), Marcel Dekker, Inc., New York, NY
    • Domenighini, M., M. Pizza, and R. Rappuoli. 1995. Bacterial ADP-ribosyltransferases, p. 59-80. In J. Moss, B. Iglewski, M. Vaughan, and A. Tu (ed.), Bacterial toxins and virulence factors in disease, 1st ed., vol.8. Marcel Dekker, Inc., New York, NY.
    • (1995) Bacterial Toxins and Virulence Factors in Disease, 1st Ed. , vol.8 , pp. 59-80
    • Domenighini, M.1    Pizza, M.2    Rappuoli, R.3
  • 13
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages
    • Domenighini, M., and R. Rappuoli. 1996. Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Mol. Microbiol. 21:667-674.
    • (1996) Mol. Microbiol. , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 14
    • 0030045743 scopus 로고    scopus 로고
    • Adherence, fibronectin binding, and induction of cytoskeleton reorganization in cultured human cells by Mycoplasma penetrans
    • Giron, J. A., M. Lange, and J. B. Baseman. 1996. Adherence, fibronectin binding, and induction of cytoskeleton reorganization in cultured human cells by Mycoplasma penetrans. Infect. Immun. 64:197-208.
    • (1996) Infect. Immun. , vol.64 , pp. 197-208
    • Giron, J.A.1    Lange, M.2    Baseman, J.B.3
  • 15
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59. (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 33749387471 scopus 로고    scopus 로고
    • A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins
    • Holbourn, K. P., C. C. Shone, and K. R. Acharya. 2006. A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins. FEBS J. 273:4579-4593.
    • (2006) FEBS J. , vol.273 , pp. 4579-4593
    • Holbourn, K.P.1    Shone, C.C.2    Acharya, K.R.3
  • 17
    • 0027519408 scopus 로고
    • NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum
    • Jung, M., I. Just, J. van Damme, J. Vandekerckhove, and K. Aktories. 1993. NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum. J. Biol. Chem. 268:23215-23218.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23215-23218
    • Jung, M.1    Just, I.2    Van Damme, J.3    Vandekerckhove, J.4    Aktories, K.5
  • 18
    • 33646271152 scopus 로고    scopus 로고
    • ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens
    • Kannan, T. R., and J. B. Baseman. 2006. ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens. Proc. Natl. Acad. Sci. USA 103:6724-6729.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6724-6729
    • Kannan, T.R.1    Baseman, J.B.2
  • 19
    • 0033788010 scopus 로고    scopus 로고
    • Hemolytic and hemoxidative activities in Mycoplasma penetrans
    • Kannan, T. R., and J. B. Baseman. 2000. Hemolytic and hemoxidative activities in Mycoplasma penetrans. Infect. Immun. 68:6419-6422.
    • (2000) Infect. Immun. , vol.68 , pp. 6419-6422
    • Kannan, T.R.1    Baseman, J.B.2
  • 20
    • 17644416114 scopus 로고    scopus 로고
    • Identification and characterization of human surfactant protein a binding protein of Mycoplasma pneumoniae
    • Kannan, T. R., D. Provenzano, J. R. Wright, and J. B. Baseman. 2005. Identification and characterization of human surfactant protein A binding protein of Mycoplasma pneumoniae. Infect. Immun. 73:2828-2834.
    • (2005) Infect. Immun. , vol.73 , pp. 2828-2834
    • Kannan, T.R.1    Provenzano, D.2    Wright, J.R.3    Baseman, J.B.4
  • 21
    • 0025718524 scopus 로고
    • Newly discovered mycoplasma isolated from patients infected with HIV
    • Lo, S. C., M. M. Hayes, R. Y. Wang, P. F. Pierce, H. Kotani, and J. W. Shih. 1991. Newly discovered mycoplasma isolated from patients infected with HIV. Lancet 338:1415-1418.
    • (1991) Lancet , vol.338 , pp. 1415-1418
    • Lo, S.C.1    Hayes, M.M.2    Wang, R.Y.3    Pierce, P.F.4    Kotani, H.5    Shih, J.W.6
  • 22
    • 0022492403 scopus 로고
    • Pertussis toxin gene: Nucleotide sequence and genetic organization
    • Locht, C., and J. M. Keith. 1986. Pertussis toxin gene: nucleotide sequence and genetic organization. Science 232:1258-1264. (Pubitemid 16066003)
    • (1986) Science , vol.232 , Issue.4755 , pp. 1258-1264
    • Locht, C.1    Keith, J.M.2
  • 24
    • 0017042555 scopus 로고
    • Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its a protomer: Possible role in the activation of adenylate cyclase
    • Moss, J., V. C. Manganiello, and M. Vaughan. 1976. Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its A protomer: possible role in the activation of adenylate cyclase. Proc. Natl. Acad. Sci. USA 73:4424-4427.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4424-4427
    • Moss, J.1    Manganiello, V.C.2    Vaughan, M.3
  • 25
    • 0035400143 scopus 로고    scopus 로고
    • An abundance of bacterial ADP-ribosyltransferases-implications for the origin of exotoxins and their human homologues
    • Pallen, M. J., A. C. Lam, N. J. Loman, and A. McBride. 2001. An abundance of bacterial ADP-ribosyltransferases-implications for the origin of exotoxins and their human homologues. Trends Microbiol. 9:302-307.
    • (2001) Trends Microbiol. , vol.9 , pp. 302-307
    • Pallen, M.J.1    Lam, A.C.2    Loman, N.J.3    McBride, A.4
  • 27
    • 63249117350 scopus 로고    scopus 로고
    • Bacterial toxins and virulence factors targeting the actin cytoskeleton and intercellular junctions
    • J. E. Alouf and M. R. Popoff (ed.), Academic Press, London, United Kingdom
    • Popoff, M. R., and B. G. Stiles. 2006. Bacterial toxins and virulence factors targeting the actin cytoskeleton and intercellular junctions, p. 154-181. In J. E. Alouf and M. R. Popoff (ed.), The comprehensive sourcebook of bacterial toxins, 3rd ed. Academic Press, London, United Kingdom.
    • (2006) The Comprehensive Sourcebook of Bacterial Toxins, 3rd Ed. , pp. 154-181
    • Popoff, M.R.1    Stiles, B.G.2
  • 28
    • 0346991736 scopus 로고    scopus 로고
    • Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis
    • Rambow-Larsen, A. A., and A. A. Weiss. 2004. Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis. J. Bacteriol. 186:43-50.
    • (2004) J. Bacteriol. , vol.186 , pp. 43-50
    • Rambow-Larsen, A.A.1    Weiss, A.A.2
  • 30
    • 0023224151 scopus 로고
    • Triton X-114 phase fractionation of an integral membrane surface protein mediating monoclonal antibody killing of Mycoplasma hyorhinis
    • Riethman, H. C., M. J. Boyer, and K. S. Wise. 1987. Triton X-114 phase fractionation of an integral membrane surface protein mediating monoclonal antibody killing of Mycoplasma hyorhinis. Infect. Immun. 55:1094-1100.
    • (1987) Infect. Immun. , vol.55 , pp. 1094-1100
    • Riethman, H.C.1    Boyer, M.J.2    Wise, K.S.3
  • 31
    • 0042324506 scopus 로고    scopus 로고
    • Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat
    • DOI 10.1021/bi034625w
    • Ritter, H., F. Koch-Nolte, V. E. Marquez, and G. E. Schulz. 2003. Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat. Biochemistry 42:10155-10162. (Pubitemid 37052034)
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10155-10162
    • Ritter, H.1    Koch-Nolte, F.2    Marquez, V.E.3    Schulz, G.E.4
  • 32
    • 0028811441 scopus 로고
    • In vitro influence of Mycoplasma penetrans on activation of peripheral T lymphocytes from healthy donors or human immunodeficiency virus-infected individuals
    • Sasaki, Y., A. Blanchard, H. L. Watson, S. Garcia, A. Dulioust, L. Montagnier, and M. L. Gougeon. 1995. In vitro influence of Mycoplasma penetrans on activation of peripheral T lymphocytes from healthy donors or human immunodeficiency virus-infected individuals. Infect. Immun. 63:4277-4283.
    • (1995) Infect. Immun. , vol.63 , pp. 4277-4283
    • Sasaki, Y.1    Blanchard, A.2    Watson, H.L.3    Garcia, S.4    Dulioust, A.5    Montagnier, L.6    Gougeon, M.L.7
  • 34
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin
    • Schering, B., M. Barmann, G. S. Chhatwal, U. Geipel, and K. Aktories. 1988. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur. J. Biochem. 171:225-229.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 225-229
    • Schering, B.1    Barmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 35
    • 0033552872 scopus 로고    scopus 로고
    • A randomized, controlled trial of a behavioral intervention to prevent sexually transmitted disease among minority women
    • Shain, R. N., J. M. Piper, E. R. Newton, S. T. Perdue, R. Ramos, J. D. Champion, and F. A. Guerra. 1999. A randomized, controlled trial of a behavioral intervention to prevent sexually transmitted disease among minority women. N. Engl. J. Med. 340:93-100.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 93-100
    • Shain, R.N.1    Piper, J.M.2    Newton, E.R.3    Perdue, S.T.4    Ramos, R.5    Champion, J.D.6    Guerra, F.A.7
  • 36
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences
    • Tatusova, T. A., and T. L. Madden. 1999. BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174:247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.