메뉴 건너뛰기




Volumn 82, Issue 7, 2014, Pages 2913-2922

Characterization of immunological cross-reactivity between enterotoxigenic Escherichia coli heat-stable toxin and human guanylin and uroguanylin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; DISULFIDE; EPITOPE; GUANYLIN; HUMAN HEAT STABLE TOXIN; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; PORCINE HEAT STABLE TOXIN; UNCLASSIFIED DRUG; UROGUANYLIN;

EID: 84903219903     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01749-14     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 33947141410 scopus 로고    scopus 로고
    • Analysis of strategies to successfully vaccinate infants in developing countries against enterotoxigenic E. coli (ETEC) disease
    • Walker RI, Steele D, Aguado T. 2007. Analysis of strategies to successfully vaccinate infants in developing countries against enterotoxigenic E. coli (ETEC) disease. Vaccine 25:2545-2566. http://dx.doi.org/10.1016/j.vaccine.2006.12.028.
    • (2007) Vaccine , vol.25 , pp. 2545-2566
    • Walker, R.I.1    Steele, D.2    Aguado, T.3
  • 2
    • 77951221998 scopus 로고    scopus 로고
    • Heat-stable enterotoxin of enterotoxigenic Escherichia coli as a vaccine target
    • Taxt A, Aasland R, Sommerfelt H, Nataro J, Puntervoll P. 2010. Heat-stable enterotoxin of enterotoxigenic Escherichia coli as a vaccine target. Infect. Immun. 78:1824-1831. http://dx.doi.org/10.1128/IAI.01397-09.
    • (2010) Infect. Immun. , vol.78 , pp. 1824-1831
    • Taxt, A.1    Aasland, R.2    Sommerfelt, H.3    Nataro, J.4    Puntervoll, P.5
  • 3
    • 80053436233 scopus 로고    scopus 로고
    • Heat-labile-and heat-stable-toxoid fusions (LTR192G-STaP13F) of human enterotoxigenic Escherichia coli elicit neutralizing antitoxin antibodies
    • Liu M, Ruan X, Zhang C, Lawson SR, Knudsen DE, Nataro JP, Robertson DC, Zhang W. 2011. Heat-labile-and heat-stable-toxoid fusions (LTR192G-STaP13F) of human enterotoxigenic Escherichia coli elicit neutralizing antitoxin antibodies. Infect. Immun. 79:4002-4009. http://dx.doi.org/10.1128/IAI.00165-11.
    • (2011) Infect. Immun. , vol.79 , pp. 4002-4009
    • Liu, M.1    Ruan, X.2    Zhang, C.3    Lawson, S.R.4    Knudsen, D.E.5    Nataro, J.P.6    Robertson, D.C.7    Zhang, W.8
  • 4
    • 73449147008 scopus 로고    scopus 로고
    • Genetic fusions of heat-labile (LT) and heat-stable (ST) toxoids of porcine enterotoxigenic Escherichia coli elicit neutralizing anti-LT and anti-STa antibodies
    • Zhang W, Zhang C, Francis DH, Fang Y, Knudsen D, Nataro JP, Robertson DC. 2010. Genetic fusions of heat-labile (LT) and heat-stable (ST) toxoids of porcine enterotoxigenic Escherichia coli elicit neutralizing anti-LT and anti-STa antibodies. Infect. Immun. 78:316-325. http://dx.doi.org/10.1128/IAI.00497-09.
    • (2010) Infect. Immun. , vol.78 , pp. 316-325
    • Zhang, W.1    Zhang, C.2    Francis, D.H.3    Fang, Y.4    Knudsen, D.5    Nataro, J.P.6    Robertson, D.C.7
  • 5
    • 84862529920 scopus 로고    scopus 로고
    • A totally synthetic lipopeptide-based self-adjuvanting vaccine induces neutralizing antibodies against heat-stable enterotoxin from enterotoxigenic Escherichia coli
    • Zeng W, Azzopardi K, Hocking D, Wong CY, Robevska G, Tauschek M, Robins-Browne RM, Jackson DC. 2012. A totally synthetic lipopeptide-based self-adjuvanting vaccine induces neutralizing antibodies against heat-stable enterotoxin from enterotoxigenic Escherichia coli. Vaccine 30:4800-4806. http://dx.doi.org/10.1016/j.vaccine.2012.05.017.
    • (2012) Vaccine , vol.30 , pp. 4800-4806
    • Zeng, W.1    Azzopardi, K.2    Hocking, D.3    Wong, C.Y.4    Robevska, G.5    Tauschek, M.6    Robins-Browne, R.M.7    Jackson, D.C.8
  • 6
    • 84871929588 scopus 로고    scopus 로고
    • Nanoparticulated heat-stable (STa) and heat-labile B subunit (LTB) recombinant toxin improves vaccine protection against enterotoxigenic Escherichia coli challenge in mouse
    • Deng G, Zeng J, Jian M, Liu W, Zhang Z, Liu X, Wang Y. 2013. Nanoparticulated heat-stable (STa) and heat-labile B subunit (LTB) recombinant toxin improves vaccine protection against enterotoxigenic Escherichia coli challenge in mouse. J. Biosci. Bioeng. 115:147-153. http://dx.doi.org/10.1016/j.jbiosc.2012.09.009.
    • (2013) J. Biosci. Bioeng. , vol.115 , pp. 147-153
    • Deng, G.1    Zeng, J.2    Jian, M.3    Liu, W.4    Zhang, Z.5    Liu, X.6    Wang, Y.7
  • 7
    • 84898892168 scopus 로고    scopus 로고
    • Characterization of heat-stable (STa) toxoids of enterotoxigenic Escherichia coli fused to a double mutant heat-labile toxin peptide in inducing neutralizing anti-STa antibodies
    • Ruan X, Robertson DC, Nataro JP, Clements JD, Zhang W. 2014. Characterization of heat-stable (STa) toxoids of enterotoxigenic Escherichia coli fused to a double mutant heat-labile toxin peptide in inducing neutralizing anti-STa antibodies. Infect. Immun. 82:1823-1832. http://dx.doi.org/10.1128/IAI.01394-13.
    • (2014) Infect. Immun. , vol.82 , pp. 1823-1832
    • Ruan, X.1    Robertson, D.C.2    Nataro, J.P.3    Clements, J.D.4    Zhang, W.5
  • 9
    • 0030696287 scopus 로고    scopus 로고
    • Occurrence, distribution, and associations of O and H serogroups, colonization factor antigens, and toxins of enterotoxigenic Escherichia coli
    • Wolf MK. 1997. Occurrence, distribution, and associations of O and H serogroups, colonization factor antigens, and toxins of enterotoxigenic Escherichia coli. Clin. Microbiol. Rev. 10:569-584.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 569-584
    • Wolf, M.K.1
  • 11
    • 0021674360 scopus 로고
    • Development of a competitive enzyme-linked immunosorbent assay (ELISA) for Escherichia coli heatstable enterotoxin (STa)
    • Lockwood DE, Robertson DC. 1984. Development of a competitive enzyme-linked immunosorbent assay (ELISA) for Escherichia coli heatstable enterotoxin (STa). J. Immunol. Methods 75:295-307. http://dx.doi.org/10.1016/0022-1759(84)90113-3.
    • (1984) J. Immunol. Methods , vol.75 , pp. 295-307
    • Lockwood, D.E.1    Robertson, D.C.2
  • 12
    • 0021056190 scopus 로고
    • Neutralization of activity of two different heat-stable enterotoxins (STh and STp) of enterotoxigenic Escherichia coli by homologous and heterologous antisera
    • Takeda T. 1983. Neutralization of activity of two different heat-stable enterotoxins (STh and STp) of enterotoxigenic Escherichia coli by homologous and heterologous antisera. FEMS Microbiol. Lett. 20:357-359. http://dx.doi.org/10.1111/j.1574-6968.1983.tb00147.x.
    • (1983) FEMS Microbiol. Lett. , vol.20 , pp. 357-359
    • Takeda, T.1
  • 13
    • 79952317126 scopus 로고    scopus 로고
    • Design and characterization of highly immunogenic heat-stable enterotoxin of enterotoxigenic Escherichia coli K99(+)
    • Aref N-EM, Saeed AM. 2011. Design and characterization of highly immunogenic heat-stable enterotoxin of enterotoxigenic Escherichia coli K99(+). J. Immunol. Methods 366:100-105. http://dx.doi.org/10.1016/j.jim.2011.01.012.
    • (2011) J. Immunol. Methods , vol.366 , pp. 100-105
    • Aref, N.-E.M.1    Saeed, A.M.2
  • 14
  • 16
    • 7044269199 scopus 로고    scopus 로고
    • Uroguanylin and guanylin peptides: pharmacology and experimental therapeutics
    • Forte LR. 2004. Uroguanylin and guanylin peptides: pharmacology and experimental therapeutics. Pharmacol. Ther. 104:137-162. http://dx.doi.org/10.1016/j.pharmthera.2004.08.007.
    • (2004) Pharmacol. Ther. , vol.104 , pp. 137-162
    • Forte, L.R.1
  • 18
    • 0025924659 scopus 로고
    • Molecular structure of the toxin domain of heat-stable enterotoxin produced by a pathogenic strain of Escherichia coli.Aputative binding site for a binding protein on rat intestinal epithelial cell membranes
    • Ozaki H, Sato T, Kubota H, Hata Y, Katsube Y, Shimonishi Y. 1991. Molecular structure of the toxin domain of heat-stable enterotoxin produced by a pathogenic strain of Escherichia coli.Aputative binding site for a binding protein on rat intestinal epithelial cell membranes. J. Biol. Chem. 266:5934-5941.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5934-5941
    • Ozaki, H.1    Sato, T.2    Kubota, H.3    Hata, Y.4    Katsube, Y.5    Shimonishi, Y.6
  • 20
    • 0027940304 scopus 로고
    • Determination of the solution structure of the peptide hormone guanylin: observation of a novel form of topological stereoisomerism
    • Skelton NJ, Garcia KC, Goeddel DV, Quan C, Burnier JP. 1994. Determination of the solution structure of the peptide hormone guanylin: observation of a novel form of topological stereoisomerism. Biochemistry 33:13581-13592. http://dx.doi.org/10.1021/bi00250a010.
    • (1994) Biochemistry , vol.33 , pp. 13581-13592
    • Skelton, N.J.1    Garcia, K.C.2    Goeddel, D.V.3    Quan, C.4    Burnier, J.P.5
  • 21
    • 20444389029 scopus 로고    scopus 로고
    • Side chain contributions to the interconversion of the topological isomers of guanylin-like peptides
    • Schulz A, Marx UC, Tidten N, Lauber T, Hidaka Y, Adermann K. 2005. Side chain contributions to the interconversion of the topological isomers of guanylin-like peptides. J. Pept. Sci. 11:319-330. http://dx.doi.org/10.1002/psc.625.
    • (2005) J. Pept. Sci. , vol.11 , pp. 319-330
    • Schulz, A.1    Marx, U.C.2    Tidten, N.3    Lauber, T.4    Hidaka, Y.5    Adermann, K.6
  • 22
    • 0035021499 scopus 로고    scopus 로고
    • Guanylin family: new intestinal peptides regulating electrolyte and water homeostasis
    • Nakazato M. 2001. Guanylin family: new intestinal peptides regulating electrolyte and water homeostasis. J. Gastroenterol. 36:219-225. http://dx.doi.org/10.1007/s005350170106.
    • (2001) J. Gastroenterol. , vol.36 , pp. 219-225
    • Nakazato, M.1
  • 23
    • 33645456128 scopus 로고    scopus 로고
    • Cellular effects of guanylin and uroguanylin
    • Sindić A, Schlatter E. 2006. Cellular effects of guanylin and uroguanylin. J. Am. Soc. Nephrol. 17:607-616. http://dx.doi.org/10.1681/ASN.2005080818.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 607-616
    • Sindić, A.1    Schlatter, E.2
  • 24
    • 0029975375 scopus 로고    scopus 로고
    • Identification of biologically active and inactive human uroguanylins in plasma and urine and their increases in renal insufficiency
    • Nakazato M, Yamaguchi H, Kinoshita H, Kangawa K, Matsuo H, Chino N, Matsukura S. 1996. Identification of biologically active and inactive human uroguanylins in plasma and urine and their increases in renal insufficiency. Biochem. Biophys. Res. Commun. 220:586-593. http://dx.doi.org/10.1006/bbrc.1996.0447.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 586-593
    • Nakazato, M.1    Yamaguchi, H.2    Kinoshita, H.3    Kangawa, K.4    Matsuo, H.5    Chino, N.6    Matsukura, S.7
  • 25
    • 50449088585 scopus 로고    scopus 로고
    • Uroguanylin, an intestinal natriuretic peptide, is delivered to the kidney as an unprocessed propeptide
    • Moss NG, Fellner RC, Qian X, Yu SJ, Li Z, Nakazato M, Goy MF. 2008. Uroguanylin, an intestinal natriuretic peptide, is delivered to the kidney as an unprocessed propeptide. Endocrinology 149:4486-4498. http://dx.doi.org/10.1210/en.2007-1725.
    • (2008) Endocrinology , vol.149 , pp. 4486-4498
    • Moss, N.G.1    Fellner, R.C.2    Qian, X.3    Yu, S.J.4    Li, Z.5    Nakazato, M.6    Goy, M.F.7
  • 26
    • 50449091751 scopus 로고    scopus 로고
    • Circulating prouroguanylin is processed to its active natriuretic form exclusively within the renal tubules
    • Qian X, Moss NG, Fellner RC, Goy MF. 2008. Circulating prouroguanylin is processed to its active natriuretic form exclusively within the renal tubules. Endocrinology 149:4499-4509. http://dx.doi.org/10.1210/en.2007-1724.
    • (2008) Endocrinology , vol.149 , pp. 4499-4509
    • Qian, X.1    Moss, N.G.2    Fellner, R.C.3    Goy, M.F.4
  • 27
    • 1842841890 scopus 로고    scopus 로고
    • Expression of the receptor guanylyl cyclase C and its ligands in reproductive tissues of the rat: a potential role for a novel signaling pathway in the epididymis
    • Jaleel M. 2002. Expression of the receptor guanylyl cyclase C and its ligands in reproductive tissues of the rat: a potential role for a novel signaling pathway in the epididymis. Biol. Reprod. 67:1975-1980. http://dx.doi.org/10.1095/biolreprod.102.006445.
    • (2002) Biol. Reprod. , vol.67 , pp. 1975-1980
    • Jaleel, M.1
  • 28
    • 81155159830 scopus 로고    scopus 로고
    • Role for the membrane receptor guanylyl cyclase-C in attention deficiency and hyperactive behavior
    • Gong R, Ding C, Hu J, Lu Y, Liu F, Mann E, Xu F, Cohen MB, Luo M. 2011. Role for the membrane receptor guanylyl cyclase-C in attention deficiency and hyperactive behavior. Science 333:1642-1646. http://dx.doi.org/10.1126/science.1207675.
    • (2011) Science , vol.333 , pp. 1642-1646
    • Gong, R.1    Ding, C.2    Hu, J.3    Lu, Y.4    Liu, F.5    Mann, E.6    Xu, F.7    Cohen, M.B.8    Luo, M.9
  • 30
  • 31
    • 0030053740 scopus 로고    scopus 로고
    • Thrombocytopenic purpura after measles, mumps and rubella vaccination: a retrospective survey by the French Regional Pharmacovigilance Centres and Pasteur-Mérieux Sérums et Vaccins
    • Jonville-Béra AP, Autret E, Galy-Eyraud C, Hessel L. 1996. Thrombocytopenic purpura after measles, mumps and rubella vaccination: a retrospective survey by the French Regional Pharmacovigilance Centres and Pasteur-Mérieux Sérums et Vaccins. Pediatr. Infect. Dis. J. 15:44-48. http://dx.doi.org/10.1097/00006454-199601000-00010.
    • (1996) Pediatr. Infect. Dis. J. , vol.15 , pp. 44-48
    • Jonville-Béra, A.P.1    Autret, E.2    Galy-Eyraud, C.3    Hessel, L.4
  • 32
    • 0030030948 scopus 로고    scopus 로고
    • Thrombocytopenia after immunization with measles vaccines: review of the vaccine adverse events reporting system (1990 to 1994)
    • Beeler J, Varricchio F, Wise R. 1996. Thrombocytopenia after immunization with measles vaccines: review of the vaccine adverse events reporting system (1990 to 1994). Pediatr. Infect. Dis. J. 15:88-90. http://dx.doi.org/10.1097/00006454-199601000-00020.
    • (1996) Pediatr. Infect. Dis. J. , vol.15 , pp. 88-90
    • Beeler, J.1    Varricchio, F.2    Wise, R.3
  • 33
    • 0014669387 scopus 로고
    • Rheumatic fever following streptococcal vaccination. Report of three cases
    • Massell BF, Honikman LH, Amezcua J. 1969. Rheumatic fever following streptococcal vaccination. Report of three cases. JAMA 207:1115-1119.
    • (1969) JAMA , vol.207 , pp. 1115-1119
    • Massell, B.F.1    Honikman, L.H.2    Amezcua, J.3
  • 36
    • 0033303533 scopus 로고    scopus 로고
    • Regulated, sidedirected secretion of proguanylin from isolated rat colonic mucosa
    • Martin S, Adermann K, Forssmann WG, Kuhn M. 1999. Regulated, sidedirected secretion of proguanylin from isolated rat colonic mucosa. Endocrinology 140:5022-5029. http://dx.doi.org/10.1210/endo.140.11.7103.
    • (1999) Endocrinology , vol.140 , pp. 5022-5029
    • Martin, S.1    Adermann, K.2    Forssmann, W.G.3    Kuhn, M.4
  • 37
    • 0030589063 scopus 로고    scopus 로고
    • A conformational epitope in the N-terminus of the Escherichia coli heat-stable enterotoxins is involved in receptor-ligand interactions
    • Garrett BM, Visweswariah SS. 1996. A conformational epitope in the N-terminus of the Escherichia coli heat-stable enterotoxins is involved in receptor-ligand interactions. Biochim. Biophys. Acta 1317:149-154. http://dx.doi.org/10.1016/S0925-4439(96)00047-6.
    • (1996) Biochim. Biophys. Acta , vol.1317 , pp. 149-154
    • Garrett, B.M.1    Visweswariah, S.S.2
  • 43
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell AD, Feig M, Brooks CL. 2004. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25:1400-1415. http://dx.doi.org/10.1002/jcc.20065.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 44
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: a Web-based graphical user interface for CHARMM
    • Jo S, Kim T, Iyer VG, Im W. 2008. CHARMM-GUI: a Web-based graphical user interface for CHARMM. J. Comput. Chem. 29:1859-1865. http://dx.doi.org/10.1002/jcc.20945.
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 45
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom J, Nordhoff E, Mirgorodskaya E, Ekman R, Roepstorff P. 1999. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34:105-116.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 46
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850-858. http://dx.doi.org/10.1021/ac950914h.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 47
    • 52649125764 scopus 로고    scopus 로고
    • Escherichia coli constructs expressing human or porcine enterotoxins induce identical diarrheal diseases in a piglet infection model
    • Zhang W, Robertson DC, Zhang C, Bai W, Zhao M, Francis DH. 2008. Escherichia coli constructs expressing human or porcine enterotoxins induce identical diarrheal diseases in a piglet infection model. Appl. Environ. Microbiol. 74:5832-5837. http://dx.doi.org/10.1128/AEM.00893-08.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5832-5837
    • Zhang, W.1    Robertson, D.C.2    Zhang, C.3    Bai, W.4    Zhao, M.5    Francis, D.H.6
  • 48
    • 0037929745 scopus 로고    scopus 로고
    • Solution structure of human proguanylin: the role of a hormone prosequence
    • Lauber T, Neudecker P, Rösch P, Marx UC. 2003. Solution structure of human proguanylin: the role of a hormone prosequence. J. Biol. Chem. 278:24118-24124. http://dx.doi.org/10.1074/jbc.M300370200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24118-24124
    • Lauber, T.1    Neudecker, P.2    Rösch, P.3    Marx, U.C.4
  • 51
    • 13444309267 scopus 로고    scopus 로고
    • Bioassay analysis using R
    • Ritz C, Streibig JC. 2005. Bioassay analysis using R. J. Stat. Softw. 12(5): 1-22. http://www.jstatsoft.org/v12/i05/paper.
    • (2005) J. Stat. Softw. , vol.12 , Issue.5 , pp. 1-22
    • Ritz, C.1    Streibig, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.