메뉴 건너뛰기




Volumn 15, Issue 11, 2013, Pages 2951-2965

Identification and characterization of two novel toxins expressed by the lethal honey bee pathogen Paenibacillus larvae, the causative agent of American foulbrood

Author keywords

[No Author keywords available]

Indexed keywords

APIS MELLIFERA; BACTERIA (MICROORGANISMS); ENTEROBACTERIACEAE; PAENIBACILLUS; PAENIBACILLUS LARVAE; PAPILIONOIDEA; POSIBACTERIA;

EID: 84886385840     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.12229     Document Type: Article
Times cited : (52)

References (60)
  • 1
    • 54149101994 scopus 로고    scopus 로고
    • Long-term global trends in crop yield and production reveal no current pollination shortage but increasing pollinator dependency
    • and ()
    • Aizen, M., Garibaldi, L., Cunningham, S., and Klein, A. (2008) Long-term global trends in crop yield and production reveal no current pollination shortage but increasing pollinator dependency. Curr Biol 18: 1572-1575.
    • (2008) Curr Biol , vol.18 , pp. 1572-1575
    • Aizen, M.1    Garibaldi, L.2    Cunningham, S.3    Klein, A.4
  • 2
    • 67349214645 scopus 로고    scopus 로고
    • The global stock of domesticated honey bees is growing slower than agricultural demand for pollination
    • and ()
    • Aizen, M.A., and Harder, L.D. (2009) The global stock of domesticated honey bees is growing slower than agricultural demand for pollination. Curr Biol 19: 915-918.
    • (2009) Curr Biol , vol.19 , pp. 915-918
    • Aizen, M.A.1    Harder, L.D.2
  • 6
    • 33745894633 scopus 로고    scopus 로고
    • Reclassification, genotypes, and virulence of Paenibacillus larvae, the etiological agent of American foulbrood in honeybees - a review
    • and ()
    • Ashiralieva, A., and Genersch, E. (2006) Reclassification, genotypes, and virulence of Paenibacillus larvae, the etiological agent of American foulbrood in honeybees - a review. Apidologie 37: 411-420.
    • (2006) Apidologie , vol.37 , pp. 411-420
    • Ashiralieva, A.1    Genersch, E.2
  • 7
    • 0032491480 scopus 로고    scopus 로고
    • Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis
    • and ()
    • Barth, H., Preiss, J.C., Hofmann, F., and Aktories, K. (1998) Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis. J Biol Chem 273: 29506-29511.
    • (1998) J Biol Chem , vol.273 , pp. 29506-29511
    • Barth, H.1    Preiss, J.C.2    Hofmann, F.3    Aktories, K.4
  • 8
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • and ()
    • Barth, H., Aktories, K., Popoff, M.R., and Stiles, B.G. (2004) Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol Mol Biol Rev 68: 373-402.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 9
    • 84855190632 scopus 로고    scopus 로고
    • The bacterium, Lysinibacillus sphaericus, as an insect pathogen
    • Berry, C. (2012) The bacterium, Lysinibacillus sphaericus, as an insect pathogen. J Invertebr Pathol 109: 1-10.
    • (2012) J Invertebr Pathol , vol.109 , pp. 1-10
    • Berry, C.1
  • 10
    • 4644305427 scopus 로고    scopus 로고
    • Two-site autoinhibition of the ADP-ribosylating mosquitocidal toxin (MTX) from Bacillus sphaericus by its 70-kDa ricin-like binding domain
    • and ()
    • Carpusca, I., Schirmer, J., and Aktories, K. (2004) Two-site autoinhibition of the ADP-ribosylating mosquitocidal toxin (MTX) from Bacillus sphaericus by its 70-kDa ricin-like binding domain. Biochemistry 43: 12009-12019.
    • (2004) Biochemistry , vol.43 , pp. 12009-12019
    • Carpusca, I.1    Schirmer, J.2    Aktories, K.3
  • 11
    • 33750015246 scopus 로고    scopus 로고
    • Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP-ribosyltransferases
    • and ()
    • Carpusca, I., Jank, T., and Aktories, K. (2006) Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP-ribosyltransferases. Mol Microbiol 62: 621-630.
    • (2006) Mol Microbiol , vol.62 , pp. 621-630
    • Carpusca, I.1    Jank, T.2    Aktories, K.3
  • 12
    • 0028304133 scopus 로고
    • Gene organization of the Streptococcus pyogenes plasmid pDB101: sequence analysis of the orf eta-copS region
    • and ()
    • Ceglowski, P., and Alonso, J.C. (1994) Gene organization of the Streptococcus pyogenes plasmid pDB101: sequence analysis of the orf eta-copS region. Gene 145: 33-39.
    • (1994) Gene , vol.145 , pp. 33-39
    • Ceglowski, P.1    Alonso, J.C.2
  • 13
    • 80052848980 scopus 로고    scopus 로고
    • Updated genome assembly and annotation of Paenibacillus larvae, the agent of American foulbrood disease of honey bees
    • Chan, Q.W.T., Cornman, R.S., Birol, I., Liao, N.Y., Chan, S.K., Docking, T.R., etal. (2011) Updated genome assembly and annotation of Paenibacillus larvae, the agent of American foulbrood disease of honey bees. BMC Genomics 12: 450.
    • (2011) BMC Genomics , vol.12 , pp. 450
    • Chan, Q.W.T.1    Cornman, R.S.2    Birol, I.3    Liao, N.Y.4    Chan, S.K.5    Docking, T.R.6
  • 15
    • 0021035805 scopus 로고
    • Medium promoting sporulation of Bacillus larvae and metabolism of medium components
    • and ()
    • Dingman, D.W., and Stahly, D.P. (1983) Medium promoting sporulation of Bacillus larvae and metabolism of medium components. Appl Environ Microbiol 46: 860-869.
    • (1983) Appl Environ Microbiol , vol.46 , pp. 860-869
    • Dingman, D.W.1    Stahly, D.P.2
  • 16
    • 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
    • and ()
    • Domenighini, M., and Rappuoli, R. (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
  • 17
    • 84858610143 scopus 로고    scopus 로고
    • Proteome analysis of Paenibacillus larvae reveals the existence of a putative S-layer protein
    • and ()
    • Fünfhaus, A., and Genersch, E. (2012) Proteome analysis of Paenibacillus larvae reveals the existence of a putative S-layer protein. Environ Microbiol Rep 4: 194-202.
    • (2012) Environ Microbiol Rep , vol.4 , pp. 194-202
    • Fünfhaus, A.1    Genersch, E.2
  • 18
    • 73749085328 scopus 로고    scopus 로고
    • Use of suppression subtractive hybridization to identify genetic differences between differentially virulent genotypes of Paenibacillus larvae, the etiological agent of American foulbrood of honeybees
    • and ()
    • Fünfhaus, A., Ashiralieva, A., Borriss, R., and Genersch, E. (2009) Use of suppression subtractive hybridization to identify genetic differences between differentially virulent genotypes of Paenibacillus larvae, the etiological agent of American foulbrood of honeybees. Environ Microbiol Rep 1: 240-250.
    • (2009) Environ Microbiol Rep , vol.1 , pp. 240-250
    • Fünfhaus, A.1    Ashiralieva, A.2    Borriss, R.3    Genersch, E.4
  • 19
    • 33846395141 scopus 로고    scopus 로고
    • Paenibacillus larvae and American foulbrood in honeybees
    • Genersch, E. (2007) Paenibacillus larvae and American foulbrood in honeybees. Berl Münch Tierärztl Wochenschr 120: 26-33.
    • (2007) Berl Münch Tierärztl Wochenschr , vol.120 , pp. 26-33
    • Genersch, E.1
  • 20
    • 73749084831 scopus 로고    scopus 로고
    • American Foulbrood in honeybees and its causative agent, Paenibacillus larvae
    • Genersch, E. (2010) American Foulbrood in honeybees and its causative agent, Paenibacillus larvae. J Invertebr Pathol 103: S10-S19.
    • (2010) J Invertebr Pathol , vol.103
    • Genersch, E.1
  • 21
    • 0038322109 scopus 로고    scopus 로고
    • The use of repetitive element PCR fingerprinting (rep-PCR) for genetic subtyping of German field isolates of Paenibacillus larvae subsp. larvae
    • and ()
    • Genersch, E., and Otten, C. (2003) The use of repetitive element PCR fingerprinting (rep-PCR) for genetic subtyping of German field isolates of Paenibacillus larvae subsp. larvae. Apidologie 34: 195-206.
    • (2003) Apidologie , vol.34 , pp. 195-206
    • Genersch, E.1    Otten, C.2
  • 22
    • 32044458387 scopus 로고    scopus 로고
    • Strain- and genotype-specific differences in virulence of Paenibacillus larvae subsp. larvae, the causative agent of American foulbrood disease in honey bees
    • and ()
    • Genersch, E., Ashiralieva, A., and Fries, I. (2005) Strain- and genotype-specific differences in virulence of Paenibacillus larvae subsp. larvae, the causative agent of American foulbrood disease in honey bees. Appl Environ Microbiol 71: 7551-7555.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7551-7555
    • Genersch, E.1    Ashiralieva, A.2    Fries, I.3
  • 23
    • 33645210665 scopus 로고    scopus 로고
    • Reclassification of Paenibacillus larvae subsp. pulvifaciens and Paenibacillus larvae subsp. larvae as Paenibacillus larvae without subspecies differentiation
    • and ()
    • Genersch, E., Forsgren, E., Pentikäinen, J., Ashiralieva, A., Rauch, S., Kilwinski, J., and Fries, I. (2006) Reclassification of Paenibacillus larvae subsp. pulvifaciens and Paenibacillus larvae subsp. larvae as Paenibacillus larvae without subspecies differentiation. Int J Syst Evol Microbiol 56: 501-511.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 501-511
    • Genersch, E.1    Forsgren, E.2    Pentikäinen, J.3    Ashiralieva, A.4    Rauch, S.5    Kilwinski, J.6    Fries, I.7
  • 24
    • 0032442562 scopus 로고    scopus 로고
    • Histopathological and histochemical changes in honeybee larvae (Apis mellifera L.) after infection with Bacillus larvae, the causative agent of American foulbrood disease
    • and ()
    • Gregorc, A., and Bowen, I.D. (1998) Histopathological and histochemical changes in honeybee larvae (Apis mellifera L.) after infection with Bacillus larvae, the causative agent of American foulbrood disease. Cell Biol Int 22: 137-144.
    • (1998) Cell Biol Int , vol.22 , pp. 137-144
    • Gregorc, A.1    Bowen, I.D.2
  • 25
    • 0033738738 scopus 로고    scopus 로고
    • Histochemical characterization of cell death in honeybee larvae midgut after treatment with Paenibacillus larvae, Amitraz and oxytetracycline
    • and ()
    • Gregorc, A., and Bowen, I.D. (2000) Histochemical characterization of cell death in honeybee larvae midgut after treatment with Paenibacillus larvae, Amitraz and oxytetracycline. Cell Biol Int 24: 319-324.
    • (2000) Cell Biol Int , vol.24 , pp. 319-324
    • Gregorc, A.1    Bowen, I.D.2
  • 26
    • 0035808303 scopus 로고    scopus 로고
    • Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis
    • and ()
    • Han, S., Arvai, A.S., Clancy, S.B., and Tainer, J.A. (2001) Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. J Mol Biol 305: 95-107.
    • (2001) J Mol Biol , vol.305 , pp. 95-107
    • Han, S.1    Arvai, A.S.2    Clancy, S.B.3    Tainer, J.A.4
  • 27
    • 0030035805 scopus 로고    scopus 로고
    • The (QxW)3 domain: a flexible lectin scaffold
    • Hazes, B. (1996) The (QxW)3 domain: a flexible lectin scaffold. Protein Sci 5: 1490-1501.
    • (1996) Protein Sci , vol.5 , pp. 1490-1501
    • Hazes, B.1
  • 28
    • 0029034935 scopus 로고
    • A mosquitocidal toxin with a ricin-like cell-binding domain
    • and ()
    • Hazes, B., and Read, R.J. (1995) A mosquitocidal toxin with a ricin-like cell-binding domain. Nat Struct Biol 2: 358-359.
    • (1995) Nat Struct Biol , vol.2 , pp. 358-359
    • Hazes, B.1    Read, R.J.2
  • 29
    • 33749387471 scopus 로고    scopus 로고
    • A family of killer toxins: exploring the mechanism of ADP-ribosylating toxins
    • and ()
    • Holbourn, K.P., Shone, C.C., and Acharya, K.R. (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
  • 31
    • 0032900248 scopus 로고    scopus 로고
    • Cytotoxic activity of pierisin, from the cabbage butterfly, Pieris rapae, in various human cancer cell lines
    • and ()
    • Kono, T., Watanabe, M., Koyama, K., Kishimoto, T., Fukushima, S., Sugimura, T., and Wakabayashi, K. (1999) Cytotoxic activity of pierisin, from the cabbage butterfly, Pieris rapae, in various human cancer cell lines. Cancer Lett 137: 75-81.
    • (1999) Cancer Lett , vol.137 , pp. 75-81
    • Kono, T.1    Watanabe, M.2    Koyama, K.3    Kishimoto, T.4    Fukushima, S.5    Sugimura, T.6    Wakabayashi, K.7
  • 32
    • 1142298587 scopus 로고    scopus 로고
    • Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42
    • Koumoutsi, A., Chen, X.-H., Henne, A., Liesegang, H., Hitzeroth, G., Franke, P., etal. (2004) Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42. J Bacteriol 186: 1084-1096.
    • (2004) J Bacteriol , vol.186 , pp. 1084-1096
    • Koumoutsi, A.1    Chen, X.-H.2    Henne, A.3    Liesegang, H.4    Hitzeroth, G.5    Franke, P.6
  • 33
    • 0038321939 scopus 로고    scopus 로고
    • Identification of glycosphingolipid receptors for Pierisin-1, a guanine-specific ADP-ribosylating toxin from the cabbage butterfly
    • Matsushima-Hibiya, Y., Watanabe, M., Hidari, K.I., Miyamoto, D., Suzuki, Y., Kasama, T., etal. (2003) Identification of glycosphingolipid receptors for Pierisin-1, a guanine-specific ADP-ribosylating toxin from the cabbage butterfly. J Biol Chem 278: 9972-9978.
    • (2003) J Biol Chem , vol.278 , pp. 9972-9978
    • Matsushima-Hibiya, Y.1    Watanabe, M.2    Hidari, K.I.3    Miyamoto, D.4    Suzuki, Y.5    Kasama, T.6
  • 34
    • 0037163040 scopus 로고    scopus 로고
    • NAD binding induces conformational changes in Rho ADP-ribosylating Clostridium botulinum C3 exoenzyme
    • Menetrey, J., Flatau, G., Stura, E.A., Charbonnier, J.B., Gas, F., Teulon, J.M., etal. (2002) NAD binding induces conformational changes in Rho ADP-ribosylating Clostridium botulinum C3 exoenzyme. J Biol Chem 277: 30950-30957.
    • (2002) J Biol Chem , vol.277 , pp. 30950-30957
    • Menetrey, J.1    Flatau, G.2    Stura, E.A.3    Charbonnier, J.B.4    Gas, F.5    Teulon, J.M.6
  • 35
    • 79960416769 scopus 로고    scopus 로고
    • Binary toxin locus analysis in Clostridium difficile
    • and ()
    • Metcalf, D.S., and Weese, J.S. (2011) Binary toxin locus analysis in Clostridium difficile. J Med Microbiol 60: 1137-1145.
    • (2011) J Med Microbiol , vol.60 , pp. 1137-1145
    • Metcalf, D.S.1    Weese, J.S.2
  • 36
    • 4344664040 scopus 로고    scopus 로고
    • Biochemical characterization of different genotypes of Paenibacillus larvae subsp. larvae, a honey bee bacterial pathogen
    • and ()
    • Neuendorf, S., Hedtke, K., Tangen, G., and Genersch, E. (2004) Biochemical characterization of different genotypes of Paenibacillus larvae subsp. larvae, a honey bee bacterial pathogen. Microbiology 150: 2381-2390.
    • (2004) Microbiology , vol.150 , pp. 2381-2390
    • Neuendorf, S.1    Hedtke, K.2    Tangen, G.3    Genersch, E.4
  • 37
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0 - remote homology modeling using structure guided sequence profiles
    • and ()
    • Nielsen, M., Lundegaard, C., Lund, O., and Petersen, T.N. (2010) CPHmodels-3.0 - remote homology modeling using structure guided sequence profiles. Nucleic Acids Res 38: W576-W581.
    • (2010) Nucleic Acids Res , vol.38
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 38
    • 77955573497 scopus 로고    scopus 로고
    • Properties and applied use of the mosquitocidal bacterium, Bacillus sphaericus
    • and ()
    • Park, H.-W., Bideshi, D.K., and Federici, B.A. (2010) Properties and applied use of the mosquitocidal bacterium, Bacillus sphaericus. J Asia Pac Entomol 13: 159-168.
    • (2010) J Asia Pac Entomol , vol.13 , pp. 159-168
    • Park, H.-W.1    Bideshi, D.K.2    Federici, B.A.3
  • 39
    • 84856972513 scopus 로고    scopus 로고
    • Heterologous expression of green fluorescent protein in Paenibacillus larvae, the causative agent of American foulbrood of honey bees
    • and ()
    • Poppinga, L., and Genersch, E. (2012) Heterologous expression of green fluorescent protein in Paenibacillus larvae, the causative agent of American foulbrood of honey bees. J Appl Microbiol 112: 430-435.
    • (2012) J Appl Microbiol , vol.112 , pp. 430-435
    • Poppinga, L.1    Genersch, E.2
  • 40
    • 84863659604 scopus 로고    scopus 로고
    • Identification and functional analysis of the S-layer protein SplA of Paenibacillus larvae, the causative agent of American foulbrood of honey bees
    • Poppinga, L., Janesch, B., Fünfhaus, A., Sekot, G., Garcia-Gonzalez, E., Hertlein, G., etal. (2012) Identification and functional analysis of the S-layer protein SplA of Paenibacillus larvae, the causative agent of American foulbrood of honey bees. PLoS Pathog 8: e1002716.
    • (2012) PLoS Pathog , vol.8
    • Poppinga, L.1    Janesch, B.2    Fünfhaus, A.3    Sekot, G.4    Garcia-Gonzalez, E.5    Hertlein, G.6
  • 41
    • 33750478363 scopus 로고    scopus 로고
    • Genome sequence of the honey bee pathogens Paenibacillus larvae and Ascosphaera apis
    • and ()
    • Qin, X., Evans, J.D., Aronstein, K.A., Murray, K.D., and Weinstock, G.M. (2006) Genome sequence of the honey bee pathogens Paenibacillus larvae and Ascosphaera apis. Insect Mol Biol 15: 715-718.
    • (2006) Insect Mol Biol , vol.15 , pp. 715-718
    • Qin, X.1    Evans, J.D.2    Aronstein, K.A.3    Murray, K.D.4    Weinstock, G.M.5
  • 42
    • 66249098546 scopus 로고    scopus 로고
    • Negative correlation between individual-insect-level virulence and colony-level virulence of Paenibacillus larvae, the etiological agent of American foulbrood of honeybees
    • and ()
    • Rauch, S., Ashiralieva, A., Hedtke, K., and Genersch, E. (2009) Negative correlation between individual-insect-level virulence and colony-level virulence of Paenibacillus larvae, the etiological agent of American foulbrood of honeybees. Appl Environ Microbiol 75: 3344-3347.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 3344-3347
    • Rauch, S.1    Ashiralieva, A.2    Hedtke, K.3    Genersch, E.4
  • 43
    • 33644825968 scopus 로고    scopus 로고
    • Structure of the mosquitocidal toxin from Bacillus sphaericus
    • and ()
    • Reinert, D.J., Carpusca, I., Aktories, K., and Schulz, G.E. (2006) Structure of the mosquitocidal toxin from Bacillus sphaericus. J Mol Biol 357: 1226-1236.
    • (2006) J Mol Biol , vol.357 , pp. 1226-1236
    • Reinert, D.J.1    Carpusca, I.2    Aktories, K.3    Schulz, G.E.4
  • 44
    • 3242775493 scopus 로고    scopus 로고
    • The PA14 domain, a conserved all-b domain in bacterial toxins, enzymes, adhesins and signaling molecules
    • and ()
    • Rigden, D.J., Mello, L.V., and Galperin, M.Y. (2004) The PA14 domain, a conserved all-b domain in bacterial toxins, enzymes, adhesins and signaling molecules. Trends Biochem Sci 29: 336-339.
    • (2004) Trends Biochem Sci , vol.29 , pp. 336-339
    • Rigden, D.J.1    Mello, L.V.2    Galperin, M.Y.3
  • 45
    • 61449109945 scopus 로고    scopus 로고
    • Bacillus sphaericus Mtx1 and Mtx2 toxins co-expressed in Escherichia coli are synergistic against Aedes aegypti larvae
    • and ()
    • Rungrod, A., Tjahaja, N.K., Soonsanga, S., Audtho, M., and Promdonkoy, B. (2009) Bacillus sphaericus Mtx1 and Mtx2 toxins co-expressed in Escherichia coli are synergistic against Aedes aegypti larvae. Biotechnol Lett 31: 551-555.
    • (2009) Biotechnol Lett , vol.31 , pp. 551-555
    • Rungrod, A.1    Tjahaja, N.K.2    Soonsanga, S.3    Audtho, M.4    Promdonkoy, B.5
  • 46
    • 0037023708 scopus 로고    scopus 로고
    • The ADP-ribosylating mosquitocidal toxin from Bacillus sphaericus - proteolytic activiation, enzyme activity,and cytotoxic effects
    • and ()
    • Schirmer, J., Just, I., and Aktories, K. (2002a) The ADP-ribosylating mosquitocidal toxin from Bacillus sphaericus - proteolytic activiation, enzyme activity, and cytotoxic effects. J Biol Chem 277: 11941-11948.
    • (2002) J Biol Chem , vol.277 , pp. 11941-11948
    • Schirmer, J.1    Just, I.2    Aktories, K.3
  • 47
    • 0036795079 scopus 로고    scopus 로고
    • Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation
    • and ()
    • Schirmer, J., Wieden, H.J., Rodnina, M.V., and Aktories, K. (2002b) Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation. Appl Environ Microbiol 68: 4894-4899.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4894-4899
    • Schirmer, J.1    Wieden, H.J.2    Rodnina, M.V.3    Aktories, K.4
  • 48
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • and ()
    • Schleberger, C., Hochmann, H., Barth, H., Aktories, K., and Schulz, G.E. (2006) Structure and action of the binary C2 toxin from Clostridium botulinum. J Mol Biol 364: 705-715.
    • (2006) J Mol Biol , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 49
    • 0025881458 scopus 로고
    • Cloning, sequencing, and expression of a gene encoding a 100-kilodalton mosquitocidal toxin from Bacillus sphaericus SSII-1
    • and ()
    • Thanabalu, T., Hindley, J., Jackson-Yap, J., and Berry, C. (1991) Cloning, sequencing, and expression of a gene encoding a 100-kilodalton mosquitocidal toxin from Bacillus sphaericus SSII-1. J Bacteriol 173: 2776-2785.
    • (1991) J Bacteriol , vol.173 , pp. 2776-2785
    • Thanabalu, T.1    Hindley, J.2    Jackson-Yap, J.3    Berry, C.4
  • 51
    • 0037225397 scopus 로고    scopus 로고
    • Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin
    • Tsuge, H., Nagahama, M., Nishimura, H., Hisatsune, J., Sakaguch, Y., Itogawa, Y., etal. (2003) Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin. J Mol Biol 325: 471-483.
    • (2003) J Mol Biol , vol.325 , pp. 471-483
    • Tsuge, H.1    Nagahama, M.2    Nishimura, H.3    Hisatsune, J.4    Sakaguch, Y.5    Itogawa, Y.6
  • 52
    • 0027992990 scopus 로고
    • Genomic fingerprinting of bacteria using repetitive sequence-based polymerase chain reaction
    • and ()
    • Versalovic, J., Schneider, M., de Bruijn, F.J., and Lupski, J.R. (1994) Genomic fingerprinting of bacteria using repetitive sequence-based polymerase chain reaction. Methods Mol Cell Biol 5: 25-40.
    • (1994) Methods Mol Cell Biol , vol.5 , pp. 25-40
    • Versalovic, J.1    Schneider, M.2    de Bruijn, F.J.3    Lupski, J.R.4
  • 53
    • 0032844523 scopus 로고    scopus 로고
    • Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: possible involvement of ADP-ribosylation in its activity
    • Watanabe, M., Kono, T., Matsushima-Hibiya, Y., Kanazawa, T., Nishisaka, N., Kishimoto, T., etal. (1999) Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: possible involvement of ADP-ribosylation in its activity. Proc Natl Acad Sci USA 96: 10608-10613.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10608-10613
    • Watanabe, M.1    Kono, T.2    Matsushima-Hibiya, Y.3    Kanazawa, T.4    Nishisaka, N.5    Kishimoto, T.6
  • 54
    • 2442666308 scopus 로고    scopus 로고
    • Enzymatic properties of Pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly
    • and ()
    • Watanabe, M., Enomoto, S., Takamura-Enya, T., Nakano, T., Koyama, K., Sugimura, T., and Wakabayashi, K. (2004) Enzymatic properties of Pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly. J Biochem 135: 471-477.
    • (2004) J Biochem , vol.135 , pp. 471-477
    • Watanabe, M.1    Enomoto, S.2    Takamura-Enya, T.3    Nakano, T.4    Koyama, K.5    Sugimura, T.6    Wakabayashi, K.7
  • 55
    • 0034875571 scopus 로고    scopus 로고
    • The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases
    • and ()
    • Wilde, C., and Aktories, K. (2001) The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases. Toxicon 39: 1647-1660.
    • (2001) Toxicon , vol.39 , pp. 1647-1660
    • Wilde, C.1    Aktories, K.2
  • 56
    • 0037022190 scopus 로고    scopus 로고
    • Structure-function analysis of the Rho-ADP-ribosylating exoenzyme C3stau2 from Staphylococcus aureus
    • and ()
    • Wilde, C., Just, I., and Aktories, K. (2002) Structure-function analysis of the Rho-ADP-ribosylating exoenzyme C3stau2 from Staphylococcus aureus. Biochemistry 41: 1529-1544.
    • (2002) Biochemistry , vol.41 , pp. 1529-1544
    • Wilde, C.1    Just, I.2    Aktories, K.3
  • 57
    • 35148880224 scopus 로고    scopus 로고
    • Mtx toxins synergize Bacillus sphaericus and Cry11Aa against susceptible and insecticide-resistant Culex quinquefasciatus larvae
    • and ()
    • Wirth, M.C., Yang, Y., Walton, W.E., Federici, B.A., and Berry, C. (2007) Mtx toxins synergize Bacillus sphaericus and Cry11Aa against susceptible and insecticide-resistant Culex quinquefasciatus larvae. Appl Environ Microbiol 73: 6066-6071.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6066-6071
    • Wirth, M.C.1    Yang, Y.2    Walton, W.E.3    Federici, B.A.4    Berry, C.5
  • 59
    • 43449115676 scopus 로고    scopus 로고
    • Fluorescence in situ-hybridization (FISH) analysis of the interactions between honeybee larvae and Paenibacillus larvae, the causative agent of American foulbrood of honeybees (Apis mellifera)
    • and ()
    • Yue, D., Nordhoff, M., Wieler, L.H., and Genersch, E. (2008) Fluorescence in situ-hybridization (FISH) analysis of the interactions between honeybee larvae and Paenibacillus larvae, the causative agent of American foulbrood of honeybees (Apis mellifera). Environ Microbiol 10: 1612-1620.
    • (2008) Environ Microbiol , vol.10 , pp. 1612-1620
    • Yue, D.1    Nordhoff, M.2    Wieler, L.H.3    Genersch, E.4
  • 60
    • 77952791624 scopus 로고    scopus 로고
    • Protein tyrosine O-glycosylation - a rather unexplored prokaryotic glycosylation system
    • and ()
    • Zarschler, K., Janesch, B., Pabst, M., Altmann, F., Messner, P., and Schäffer, C. (2010) Protein tyrosine O-glycosylation - a rather unexplored prokaryotic glycosylation system. Glycobiology 20: 787-798.
    • (2010) Glycobiology , vol.20 , pp. 787-798
    • Zarschler, K.1    Janesch, B.2    Pabst, M.3    Altmann, F.4    Messner, P.5    Schäffer, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.