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Volumn 57, Issue 4, 2011, Pages 525-539

Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces Cerevisiae

Author keywords

Apoptosis; E. coli O157:H7; Ribosome depurination; Ribosome inactivating protein; Ricin; Shiga toxin

Indexed keywords

ALPHA SARCIN; ARGININE; ASPARAGINE; GLUTAMIC ACID; RIBOSOME RNA; TYROSINE; VEROTOXIN 1; VEROTOXIN 2;

EID: 79952359595     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2010.12.006     Document Type: Article
Times cited : (19)

References (54)
  • 1
    • 33847383363 scopus 로고    scopus 로고
    • The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity
    • Baykal U., Tumer N.E. The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity. Plant J. 2007, 49:995-1007.
    • (2007) Plant J. , vol.49 , pp. 995-1007
    • Baykal, U.1    Tumer, N.E.2
  • 2
    • 0030721959 scopus 로고    scopus 로고
    • The RNA-N-glycosidase activity of Shiga-like toxin I: kinetic parameters of the native and activated toxin
    • Brigotti M., Carnicelli D., Alvergna P., Mazzaracchio R., Sperti S., Montanaro L. The RNA-N-glycosidase activity of Shiga-like toxin I: kinetic parameters of the native and activated toxin. Toxicon 1997, 35:1431-1437.
    • (1997) Toxicon , vol.35 , pp. 1431-1437
    • Brigotti, M.1    Carnicelli, D.2    Alvergna, P.3    Mazzaracchio, R.4    Sperti, S.5    Montanaro, L.6
  • 3
    • 0028024682 scopus 로고
    • Construction of mutant genes for a non-toxic verotoxin 2 variant (VT2vp1) of Escherichia coli and characterization of purified mutant toxins
    • Cao C., Kurazono H., Yamasaki S., Kashiwagi K., Igarashi K., Takeda Y. Construction of mutant genes for a non-toxic verotoxin 2 variant (VT2vp1) of Escherichia coli and characterization of purified mutant toxins. Microbiol. Immunol. 1994, 38:441-447.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 441-447
    • Cao, C.1    Kurazono, H.2    Yamasaki, S.3    Kashiwagi, K.4    Igarashi, K.5    Takeda, Y.6
  • 4
    • 56749154533 scopus 로고    scopus 로고
    • The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae
    • Chiou J.C., Li X.P., Remacha M., Ballesta J.P., Tumer N.E. The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae. Mol. Microbiol. 2008, 70:1441-1452.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1441-1452
    • Chiou, J.C.1    Li, X.P.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 6
    • 0027494536 scopus 로고
    • The role of tyrosine-114 in the enzymatic activity of the Shiga-like toxin I A-chain
    • Deresiewicz R.L., Austin P.R., Hovde C.J. The role of tyrosine-114 in the enzymatic activity of the Shiga-like toxin I A-chain. Mol. Gen. Genet. 1993, 241:467-473.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 467-473
    • Deresiewicz, R.L.1    Austin, P.R.2    Hovde, C.J.3
  • 7
    • 0023854742 scopus 로고
    • Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins
    • Endo Y., Tsurugi K., Yutsudo T., Takeda Y., Ogasawara T., Igarashi K. Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. Eur. J. Biochem. 1988, 171:45-50.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 45-50
    • Endo, Y.1    Tsurugi, K.2    Yutsudo, T.3    Takeda, Y.4    Ogasawara, T.5    Igarashi, K.6
  • 8
    • 0028367338 scopus 로고
    • Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution
    • Fraser M.E., Chernaia M.M., Kozlov Y.V., James M.N. Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution. Nat. Struct. Biol. 1994, 1:59-64.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 59-64
    • Fraser, M.E.1    Chernaia, M.M.2    Kozlov, Y.V.3    James, M.N.4
  • 11
    • 0028961149 scopus 로고
    • Furin-induced cleavage and activation of Shiga toxin
    • Garred O., van Deurs B., Sandvig K. Furin-induced cleavage and activation of Shiga toxin. J. Biol. Chem. 1995, 270:10817-10821.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10817-10821
    • Garred, O.1    van Deurs, B.2    Sandvig, K.3
  • 12
    • 0025878152 scopus 로고
    • Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits. Evidence for B subunit modulation of a subunit function
    • Head S.C., Karmali M.A., Lingwood C.A. Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits. Evidence for B subunit modulation of a subunit function. J. Biol. Chem. 1991, 266:3617-3621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3617-3621
    • Head, S.C.1    Karmali, M.A.2    Lingwood, C.A.3
  • 14
    • 4043177111 scopus 로고    scopus 로고
    • Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity
    • Hudak K.A., Parikh B.A., Di R., Baricevic M., Santana M., Seskar M., Tumer N.E. Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity. Nucleic Acids Res. 2004, 32:4244-4256.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4244-4256
    • Hudak, K.A.1    Parikh, B.A.2    Di, R.3    Baricevic, M.4    Santana, M.5    Seskar, M.6    Tumer, N.E.7
  • 15
    • 0029160529 scopus 로고
    • Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity
    • Hur Y., Hwang D.J., Zoubenko O., Coetzer C., Uckun F.M., Tumer N.E. Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity. Proc. Natl. Acad. Sci. U S A. 1995, 92:8448-8452.
    • (1995) Proc. Natl. Acad. Sci. U S A. , vol.92 , pp. 8448-8452
    • Hur, Y.1    Hwang, D.J.2    Zoubenko, O.3    Coetzer, C.4    Uckun, F.M.5    Tumer, N.E.6
  • 16
    • 0022508584 scopus 로고
    • Pathogenesis of Shigella diarrhea. XI. Isolation of a Shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
    • Jacewicz M., Clausen H., Nudelman E., Donohue-Rolfe A., Keusch G.T. Pathogenesis of Shigella diarrhea. XI. Isolation of a Shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide. J. Exp. Med. 1986, 163:1391-1404.
    • (1986) J. Exp. Med. , vol.163 , pp. 1391-1404
    • Jacewicz, M.1    Clausen, H.2    Nudelman, E.3    Donohue-Rolfe, A.4    Keusch, G.T.5
  • 17
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins-from cell biology to biomedical applications
    • Johannes L., Romer W. Shiga toxins-from cell biology to biomedical applications. Nat. Rev. Microbiol. 2010, 8:105-116.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 105-116
    • Johannes, L.1    Romer, W.2
  • 19
    • 33745090478 scopus 로고    scopus 로고
    • The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins
    • Korennykh A.V., Piccirilli J.A., Correll C.C. The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nat. Struct. Mol. Biol. 2006, 13:436-443.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 436-443
    • Korennykh, A.V.1    Piccirilli, J.A.2    Correll, C.C.3
  • 20
    • 34548348189 scopus 로고    scopus 로고
    • Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
    • Korennykh A.V., Correll C.C., Piccirilli J.A. Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 2007, 13:1391-1396.
    • (2007) RNA , vol.13 , pp. 1391-1396
    • Korennykh, A.V.1    Correll, C.C.2    Piccirilli, J.A.3
  • 21
    • 20744449290 scopus 로고    scopus 로고
    • A role for the protease-sensitive loop region of Shiga-like toxin 1 in the retrotranslocation of its A1 domain from the endoplasmic reticulum lumen
    • LaPointe P., Wei X., Gariepy J. A role for the protease-sensitive loop region of Shiga-like toxin 1 in the retrotranslocation of its A1 domain from the endoplasmic reticulum lumen. J. Biol. Chem. 2005, 280:23310-23318.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23310-23318
    • LaPointe, P.1    Wei, X.2    Gariepy, J.3
  • 22
    • 0000243829 scopus 로고
    • PROCHECK- a program to check the sterochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK- a program to check the sterochemical quality of protein structures. J. App. Cryst. 1993, 26:283-291.
    • (1993) J. App. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 1971, 55:379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 24
    • 38849180895 scopus 로고    scopus 로고
    • Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells
    • Lee S.Y., Lee M.S., Cherla R.P., Tesh V.L. Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells. Cell. Microbiol. 2008, 10:770-780.
    • (2008) Cell. Microbiol. , vol.10 , pp. 770-780
    • Lee, S.Y.1    Lee, M.S.2    Cherla, R.P.3    Tesh, V.L.4
  • 25
    • 33845976010 scopus 로고    scopus 로고
    • Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae
    • Li X.P., Baricevic M., Saidasan H., Tumer N.E. Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae. Infect. Immun. 2007, 75:417-428.
    • (2007) Infect. Immun. , vol.75 , pp. 417-428
    • Li, X.P.1    Baricevic, M.2    Saidasan, H.3    Tumer, N.E.4
  • 26
    • 66149084818 scopus 로고    scopus 로고
    • A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes
    • Li X.P., Chiou J.C., Remacha M., Ballesta J.P., Tumer N.E. A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes. Biochemistry 2009, 48:3853-3863.
    • (2009) Biochemistry , vol.48 , pp. 3853-3863
    • Li, X.P.1    Chiou, J.C.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 28
    • 33750684296 scopus 로고    scopus 로고
    • Don't eat the spinach-controlling foodborne infectious disease
    • Maki D.G. Don't eat the spinach-controlling foodborne infectious disease. N. Engl. J. Med. 2006, 355:1952-1955.
    • (2006) N. Engl. J. Med. , vol.355 , pp. 1952-1955
    • Maki, D.G.1
  • 29
    • 41249097425 scopus 로고    scopus 로고
    • The catalytic subunit of shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain
    • McCluskey A.J., Poon G.M., Bolewska-Pedyczak E., Srikumar T., Jeram S.M., Raught B., Gariepy J. The catalytic subunit of shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain. J. Mol. Biol. 2008, 378:375-386.
    • (2008) J. Mol. Biol. , vol.378 , pp. 375-386
    • McCluskey, A.J.1    Poon, G.M.2    Bolewska-Pedyczak, E.3    Srikumar, T.4    Jeram, S.M.5    Raught, B.6    Gariepy, J.7
  • 30
    • 0032854066 scopus 로고    scopus 로고
    • Regulated expression of the Shiga toxin B gene induces apoptosis in mammalian fibroblastic cells
    • Nakagawa I., Nakata M., Kawabata S., Hamada S. Regulated expression of the Shiga toxin B gene induces apoptosis in mammalian fibroblastic cells. Mol. Microbiol. 1999, 33:1190-1199.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1190-1199
    • Nakagawa, I.1    Nakata, M.2    Kawabata, S.3    Hamada, S.4
  • 34
    • 0027486751 scopus 로고
    • Characterization of non-toxic mutant toxins of Vero toxin 1 that were constructed by replacing amino acids in the A subunit
    • Ohmura M., Yamasaki S., Kurazono H., Kashiwagi K., Igarashi K., Takeda Y. Characterization of non-toxic mutant toxins of Vero toxin 1 that were constructed by replacing amino acids in the A subunit. Microb. Pathog. 1993, 15:169-176.
    • (1993) Microb. Pathog. , vol.15 , pp. 169-176
    • Ohmura, M.1    Yamasaki, S.2    Kurazono, H.3    Kashiwagi, K.4    Igarashi, K.5    Takeda, Y.6
  • 35
    • 0036828767 scopus 로고    scopus 로고
    • Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the alpha-sarcin/ricin loop of rRNA
    • Parikh B.A., Coetzer C., Tumer N.E. Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the alpha-sarcin/ricin loop of rRNA. J. Biol. Chem. 2002, 277:41428-41437.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41428-41437
    • Parikh, B.A.1    Coetzer, C.2    Tumer, N.E.3
  • 36
    • 14044259392 scopus 로고    scopus 로고
    • Evidence for retro-translocation of pokeweed antiviral protein from endoplasmic reticulum into cytosol and separation of its activity on ribosomes from its activity on capped RNA
    • Parikh B.A., Baykal U., Di R., Tumer N.E. Evidence for retro-translocation of pokeweed antiviral protein from endoplasmic reticulum into cytosol and separation of its activity on ribosomes from its activity on capped RNA. Biochemistry 2005, 44:2478-2490.
    • (2005) Biochemistry , vol.44 , pp. 2478-2490
    • Parikh, B.A.1    Baykal, U.2    Di, R.3    Tumer, N.E.4
  • 37
    • 44449144592 scopus 로고    scopus 로고
    • Ricin inhibits activation of the unfolded protein response by preventing splicing of the HAC1 mRNA
    • Parikh B.A., Tortora A., Li X.P., Tumer N.E. Ricin inhibits activation of the unfolded protein response by preventing splicing of the HAC1 mRNA. J. Biol. Chem. 2008, 283:6145-6153.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6145-6153
    • Parikh, B.A.1    Tortora, A.2    Li, X.P.3    Tumer, N.E.4
  • 38
    • 0031848112 scopus 로고    scopus 로고
    • Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections
    • Paton J.C., Paton A.W. Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections. Clin. Microbiol. Rev. 1998, 11:450-479.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 450-479
    • Paton, J.C.1    Paton, A.W.2
  • 39
    • 0028270884 scopus 로고
    • Hemolytic-uremic syndrome and enterohemorrhagic Escherichia coli
    • quiz 476
    • Pickering L.K., Obrig T.G., Stapleton F.B. Hemolytic-uremic syndrome and enterohemorrhagic Escherichia coli. Pediatr. Infect. Dis. J. 1994, 13:459-475. quiz 476.
    • (1994) Pediatr. Infect. Dis. J. , vol.13 , pp. 459-475
    • Pickering, L.K.1    Obrig, T.G.2    Stapleton, F.B.3
  • 40
    • 0025034728 scopus 로고
    • Rapid and specific detection of verotoxin genes in Escherichia coli by the polymerase chain reaction
    • Pollard D.R., Johnson W.M., Lior H., Tyler S.D., Rozee K.R. Rapid and specific detection of verotoxin genes in Escherichia coli by the polymerase chain reaction. J. Clin. Microbiol. 1990, 28:540-545.
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 540-545
    • Pollard, D.R.1    Johnson, W.M.2    Lior, H.3    Tyler, S.D.4    Rozee, K.R.5
  • 41
    • 0034603171 scopus 로고    scopus 로고
    • Modeling and alanine scanning mutagenesis studies of recombinant pokeweed antiviral protein
    • Rajamohan F., Pugmire M.J., Kurinov I.V., Uckun F.M. Modeling and alanine scanning mutagenesis studies of recombinant pokeweed antiviral protein. J. Biol. Chem. 2000, 275:3382-3390.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3382-3390
    • Rajamohan, F.1    Pugmire, M.J.2    Kurinov, I.V.3    Uckun, F.M.4
  • 43
    • 0025986909 scopus 로고
    • Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action
    • Ready M.P., Kim Y., Robertus J.D. Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action. Proteins 1991, 10:270-278.
    • (1991) Proteins , vol.10 , pp. 270-278
    • Ready, M.P.1    Kim, Y.2    Robertus, J.D.3
  • 44
    • 0022328790 scopus 로고
    • Calculation of molecular volumes and areas for structures of known geometry
    • Richards F.M. Calculation of molecular volumes and areas for structures of known geometry. Methods Enzymol. 1985, 115:440-464.
    • (1985) Methods Enzymol. , vol.115 , pp. 440-464
    • Richards, F.M.1
  • 45
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: lessons learned from plant and bacterial toxins
    • Sandvig K., van Deurs B. Delivery into cells: lessons learned from plant and bacterial toxins. Gene Ther. 2005, 12:865-872.
    • (2005) Gene Ther. , vol.12 , pp. 865-872
    • Sandvig, K.1    van Deurs, B.2
  • 47
  • 48
    • 17144365102 scopus 로고    scopus 로고
    • Hemolytic uremic syndrome; pathogenesis, treatment, and outcome
    • Siegler R., Oakes R. Hemolytic uremic syndrome; pathogenesis, treatment, and outcome. Curr. Opin. Pediatr. 2005, 17:200-204.
    • (2005) Curr. Opin. Pediatr. , vol.17 , pp. 200-204
    • Siegler, R.1    Oakes, R.2
  • 50
    • 0032879634 scopus 로고    scopus 로고
    • Ricin A chain utilizes the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
    • Simpson J.C., Roberts L.M., Romisch K., Davey J., Wolf D.H., Lord J.M. Ricin A chain utilizes the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast. FEBS Lett. 1999, 459:80-84.
    • (1999) FEBS Lett. , vol.459 , pp. 80-84
    • Simpson, J.C.1    Roberts, L.M.2    Romisch, K.3    Davey, J.4    Wolf, D.H.5    Lord, J.M.6
  • 51
    • 67650096429 scopus 로고    scopus 로고
    • Monoclonal antibody 11E10, which neutralizes shiga toxin type 2 (Stx2), recognizes three regions on the Stx2 A subunit, blocks the enzymatic action of the toxin in vitro, and alters the overall cellular distribution of the toxin
    • Smith M.J., Melton-Celsa A.R., Sinclair J.F., Carvalho H.M., Robinson C.M., O'Brien A.D. Monoclonal antibody 11E10, which neutralizes shiga toxin type 2 (Stx2), recognizes three regions on the Stx2 A subunit, blocks the enzymatic action of the toxin in vitro, and alters the overall cellular distribution of the toxin. Infect. Immun. 2009, 77:2730-2740.
    • (2009) Infect. Immun. , vol.77 , pp. 2730-2740
    • Smith, M.J.1    Melton-Celsa, A.R.2    Sinclair, J.F.3    Carvalho, H.M.4    Robinson, C.M.5    O'Brien, A.D.6
  • 52
    • 0032412288 scopus 로고    scopus 로고
    • Disruption of an internal membrane-spanning region in Shiga toxin 1 reduces cytotoxicity
    • Suhan M.L., Hovde C.J. Disruption of an internal membrane-spanning region in Shiga toxin 1 reduces cytotoxicity. Infect. Immun. 1998, 66:5252-5259.
    • (1998) Infect. Immun. , vol.66 , pp. 5252-5259
    • Suhan, M.L.1    Hovde, C.J.2
  • 54
    • 0024299352 scopus 로고
    • Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2
    • Waddell T., Head S., Petric M., Cohen A., Lingwood C. Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2. Biochem. Biophys. Res. Commun. 1988, 152:674-679.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 674-679
    • Waddell, T.1    Head, S.2    Petric, M.3    Cohen, A.4    Lingwood, C.5


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