메뉴 건너뛰기




Volumn 130, Issue , 2016, Pages 94-107

Growth phase-dependent composition of the Helicobacter pylori exoproteome

Author keywords

Autolysis; Autotransporter; Bacterial protein secretion; Exoproteome; Gastric cancer; Mass spectrometry; Outer membrane vesicles; Peptic ulcer disease; Proteomics; Secretome; VacA

Indexed keywords

BACTERIAL PROTEIN; EXOPROTEOME; OUTER MEMBRANE PROTEIN; PROTEOME; UNCLASSIFIED DRUG; VACUOLATING TOXIN; SIGNAL PEPTIDE; VACA PROTEIN, HELICOBACTER PYLORI;

EID: 84946422885     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2015.08.025     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0024316918 scopus 로고
    • Prevalence of Helicobacter pylori infection and histologic gastritis in asymptomatic persons
    • Dooley C.P., Cohen H., Fitzgibbons P.L., Bauer M., Appleman M.D., Perez-Perez G.I., et al. Prevalence of Helicobacter pylori infection and histologic gastritis in asymptomatic persons. N. Engl. J. Med. 1989, 321(23):1562-1566.
    • (1989) N. Engl. J. Med. , vol.321 , Issue.23 , pp. 1562-1566
    • Dooley, C.P.1    Cohen, H.2    Fitzgibbons, P.L.3    Bauer, M.4    Appleman, M.D.5    Perez-Perez, G.I.6
  • 3
    • 33750075748 scopus 로고    scopus 로고
    • Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses
    • Algood H.M., Cover T.L. Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses. Clin. Microbiol. Rev. 2006, 19(4):597-613.
    • (2006) Clin. Microbiol. Rev. , vol.19 , Issue.4 , pp. 597-613
    • Algood, H.M.1    Cover, T.L.2
  • 4
    • 0037057683 scopus 로고    scopus 로고
    • Helicobacter pylori infection
    • Suerbaum S., Michetti P. Helicobacter pylori infection. N. Engl. J. Med. 2002, 347(15):1175-1186.
    • (2002) N. Engl. J. Med. , vol.347 , Issue.15 , pp. 1175-1186
    • Suerbaum, S.1    Michetti, P.2
  • 5
    • 65449190100 scopus 로고    scopus 로고
    • Helicobacter pylori in health and disease
    • Cover T.L., Blaser M.J. Helicobacter pylori in health and disease. Gastroenterology 2009, 136(6):1863-1873.
    • (2009) Gastroenterology , vol.136 , Issue.6 , pp. 1863-1873
    • Cover, T.L.1    Blaser, M.J.2
  • 6
    • 84893734333 scopus 로고    scopus 로고
    • Structural and functional aspects of the Helicobacter pylori secretome
    • Zanotti G., Cendron L. Structural and functional aspects of the Helicobacter pylori secretome. World J. Gastroenterol. 2014, 20(6):1402-1423.
    • (2014) World J. Gastroenterol. , vol.20 , Issue.6 , pp. 1402-1423
    • Zanotti, G.1    Cendron, L.2
  • 7
    • 0030021824 scopus 로고    scopus 로고
    • Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis
    • Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M., Connors J.B., et al. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect. Immun. 1996, 64(3):905-912.
    • (1996) Infect. Immun. , vol.64 , Issue.3 , pp. 905-912
    • Phadnis, S.H.1    Parlow, M.H.2    Levy, M.3    Ilver, D.4    Caulkins, C.M.5    Connors, J.B.6
  • 8
    • 0036089516 scopus 로고    scopus 로고
    • Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori
    • Bumann D., Aksu S., Wendland M., Janek K., Zimny-Arndt U., Sabarth N., et al. Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori. Infect. Immun. 2002, 70(7):3396-3403.
    • (2002) Infect. Immun. , vol.70 , Issue.7 , pp. 3396-3403
    • Bumann, D.1    Aksu, S.2    Wendland, M.3    Janek, K.4    Zimny-Arndt, U.5    Sabarth, N.6
  • 10
    • 34447545490 scopus 로고    scopus 로고
    • Direct analysis of the extracellular proteome from two strains of Helicobacter pylori
    • Smith T.G., Lim J.M., Weinberg M.V., Wells L., Hoover T.R. Direct analysis of the extracellular proteome from two strains of Helicobacter pylori. Proteomics 2007, 7(13):2240-2245.
    • (2007) Proteomics , vol.7 , Issue.13 , pp. 2240-2245
    • Smith, T.G.1    Lim, J.M.2    Weinberg, M.V.3    Wells, L.4    Hoover, T.R.5
  • 12
    • 78649977975 scopus 로고    scopus 로고
    • Uptake of Helicobacter pylori outer membrane vesicles by gastric epithelial cells
    • Parker H., Chitcholtan K., Hampton M.B., Keenan J.I. Uptake of Helicobacter pylori outer membrane vesicles by gastric epithelial cells. Infect. Immun. 2010, 78(12):5054-5061.
    • (2010) Infect. Immun. , vol.78 , Issue.12 , pp. 5054-5061
    • Parker, H.1    Chitcholtan, K.2    Hampton, M.B.3    Keenan, J.I.4
  • 13
    • 0031911053 scopus 로고    scopus 로고
    • Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
    • Vanet A., Labigne A. Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins. Infect. Immun. 1998, 66(3):1023-1027.
    • (1998) Infect. Immun. , vol.66 , Issue.3 , pp. 1023-1027
    • Vanet, A.1    Labigne, A.2
  • 16
    • 84858226117 scopus 로고    scopus 로고
    • Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro
    • Jimenez-Soto L.F., Rohrer S., Jain U., Ertl C., Sewald X., Haas R. Effects of cholesterol on Helicobacter pylori growth and virulence properties in vitro. Helicobacter 2012, 17(2):133-139.
    • (2012) Helicobacter , vol.17 , Issue.2 , pp. 133-139
    • Jimenez-Soto, L.F.1    Rohrer, S.2    Jain, U.3    Ertl, C.4    Sewald, X.5    Haas, R.6
  • 17
    • 84902007682 scopus 로고    scopus 로고
    • Analysis of surface-exposed outer membrane proteins in Helicobacter pylori
    • Voss B.J., Gaddy J.A., McDonald W.H., Cover T.L. Analysis of surface-exposed outer membrane proteins in Helicobacter pylori. J. Bacteriol. 2014, 196(13):2455-2471.
    • (2014) J. Bacteriol. , vol.196 , Issue.13 , pp. 2455-2471
    • Voss, B.J.1    Gaddy, J.A.2    McDonald, W.H.3    Cover, T.L.4
  • 18
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68(5):850-858.
    • (1996) Anal. Chem. , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 19
    • 84945313880 scopus 로고    scopus 로고
    • Supporting data for analysis of the Helicobacter pylori exoproteome
    • (in press)
    • Snider C.A., Voss B.J., McDonald W.H., Cover T.L. Supporting data for analysis of the Helicobacter pylori exoproteome. Data Brief 2015, (in press).
    • (2015) Data Brief
    • Snider, C.A.1    Voss, B.J.2    McDonald, W.H.3    Cover, T.L.4
  • 20
    • 0037311919 scopus 로고    scopus 로고
    • TM4: a free, open-source system for microarray data management and analysis
    • Saeed A.I., Sharov V., White J., Li J., Liang W., Bhagabati N., et al. TM4: a free, open-source system for microarray data management and analysis. Biotechniques 2003, 34(2):374-378.
    • (2003) Biotechniques , vol.34 , Issue.2 , pp. 374-378
    • Saeed, A.I.1    Sharov, V.2    White, J.3    Li, J.4    Liang, W.5    Bhagabati, N.6
  • 21
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8(10):785-786.
    • (2011) Nat. Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 22
    • 0026739795 scopus 로고
    • Purification and characterization of the vacuolating toxin from Helicobacter pylori
    • Cover T.L., Blaser M.J. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J. Biol. Chem. 1992, 267(15):10570-10575.
    • (1992) J. Biol. Chem. , vol.267 , Issue.15 , pp. 10570-10575
    • Cover, T.L.1    Blaser, M.J.2
  • 23
    • 34247594931 scopus 로고    scopus 로고
    • Inhibition of T-cell proliferation by Helicobacter pylori gamma-glutamyl transpeptidase
    • Schmees C., Prinz C., Treptau T., Rad R., Hengst L., Voland P., et al. Inhibition of T-cell proliferation by Helicobacter pylori gamma-glutamyl transpeptidase. Gastroenterology 2007, 132(5):1820-1833.
    • (2007) Gastroenterology , vol.132 , Issue.5 , pp. 1820-1833
    • Schmees, C.1    Prinz, C.2    Treptau, T.3    Rad, R.4    Hengst, L.5    Voland, P.6
  • 24
    • 84870949997 scopus 로고    scopus 로고
    • Secreted protein HP1286 of Helicobacter pylori strain 26695 induces apoptosis of AGS cells
    • Li J., Meng F.L., He L.H., Zhang J.Z. Secreted protein HP1286 of Helicobacter pylori strain 26695 induces apoptosis of AGS cells. Biomed. Environ. Sci. 2012, 25(6):614-619.
    • (2012) Biomed. Environ. Sci. , vol.25 , Issue.6 , pp. 614-619
    • Li, J.1    Meng, F.L.2    He, L.H.3    Zhang, J.Z.4
  • 25
    • 17844399575 scopus 로고    scopus 로고
    • The secreted peptidyl prolyl cis,trans-isomerase HP0175 of Helicobacter pylori induces apoptosis of gastric epithelial cells in a TLR4- and apoptosis signal-regulating kinase 1-dependent manner
    • Basak C., Pathak S.K., Bhattacharyya A., Pathak S., Basu J., Kundu M. The secreted peptidyl prolyl cis,trans-isomerase HP0175 of Helicobacter pylori induces apoptosis of gastric epithelial cells in a TLR4- and apoptosis signal-regulating kinase 1-dependent manner. J. Immunol. 2005, 174(9):5672-5680.
    • (2005) J. Immunol. , vol.174 , Issue.9 , pp. 5672-5680
    • Basak, C.1    Pathak, S.K.2    Bhattacharyya, A.3    Pathak, S.4    Basu, J.5    Kundu, M.6
  • 26
    • 77957232471 scopus 로고    scopus 로고
    • Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion
    • Hoy B., Lower M., Weydig C., Carra G., Tegtmeyer N., Geppert T., et al. Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion. EMBO Rep. 2010, 11(10):798-804.
    • (2010) EMBO Rep. , vol.11 , Issue.10 , pp. 798-804
    • Hoy, B.1    Lower, M.2    Weydig, C.3    Carra, G.4    Tegtmeyer, N.5    Geppert, T.6
  • 27
    • 0028355422 scopus 로고
    • Gene structure of the Helicobacter pylori cytotoxin and evidence of its key role in gastric disease
    • Telford J.L., Ghiara P., Dell'Orco M., Comanducci M., Burroni D., Bugnoli M., et al. Gene structure of the Helicobacter pylori cytotoxin and evidence of its key role in gastric disease. J. Exp. Med. 1994, 179(5):1653-1658.
    • (1994) J. Exp. Med. , vol.179 , Issue.5 , pp. 1653-1658
    • Telford, J.L.1    Ghiara, P.2    Dell'Orco, M.3    Comanducci, M.4    Burroni, D.5    Bugnoli, M.6
  • 28
    • 0035158890 scopus 로고    scopus 로고
    • Carboxy-terminal proteolytic processing of Helicobacter pylori vacuolating toxin
    • Nguyen V.Q., Caprioli R.M., Cover T.L. Carboxy-terminal proteolytic processing of Helicobacter pylori vacuolating toxin. Infect. Immun. 2001, 69(1):543-546.
    • (2001) Infect. Immun. , vol.69 , Issue.1 , pp. 543-546
    • Nguyen, V.Q.1    Caprioli, R.M.2    Cover, T.L.3
  • 29
    • 0034085068 scopus 로고    scopus 로고
    • Intercellular communication in Helicobacter pylori: luxS is essential for the production of an extracellular signaling molecule
    • Forsyth M.H., Cover T.L. Intercellular communication in Helicobacter pylori: luxS is essential for the production of an extracellular signaling molecule. Infect. Immun. 2000, 68(6):3193-3199.
    • (2000) Infect. Immun. , vol.68 , Issue.6 , pp. 3193-3199
    • Forsyth, M.H.1    Cover, T.L.2
  • 30
    • 0034783458 scopus 로고    scopus 로고
    • Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori
    • Fischer W., Buhrdorf R., Gerland E., Haas R. Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori. Infect. Immun. 2001, 69(11):6769-6775.
    • (2001) Infect. Immun. , vol.69 , Issue.11 , pp. 6769-6775
    • Fischer, W.1    Buhrdorf, R.2    Gerland, E.3    Haas, R.4
  • 32
    • 84866648509 scopus 로고    scopus 로고
    • Multiple pathways of plasmid DNA transfer in Helicobacter pylori
    • Rohrer S., Holsten L., Weiss E., Benghezal M., Fischer W., Haas R. Multiple pathways of plasmid DNA transfer in Helicobacter pylori. PLoS One 2012, 7(9):e45623.
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e45623
    • Rohrer, S.1    Holsten, L.2    Weiss, E.3    Benghezal, M.4    Fischer, W.5    Haas, R.6
  • 33
    • 0035725211 scopus 로고    scopus 로고
    • Systematic mutagenesis of the Helicobacter pylori cag pathogenicity island: essential genes for CagA translocation in host cells and induction of interleukin-8
    • Fischer W., Puls J., Buhrdorf R., Gebert B., Odenbreit S., Haas R. Systematic mutagenesis of the Helicobacter pylori cag pathogenicity island: essential genes for CagA translocation in host cells and induction of interleukin-8. Mol. Microbiol. 2001, 42(5):1337-1348.
    • (2001) Mol. Microbiol. , vol.42 , Issue.5 , pp. 1337-1348
    • Fischer, W.1    Puls, J.2    Buhrdorf, R.3    Gebert, B.4    Odenbreit, S.5    Haas, R.6
  • 34
    • 0031866651 scopus 로고    scopus 로고
    • Extracellular release of antigenic proteins by Helicobacter pylori
    • Cao P., McClain M.S., Forsyth M.H., Cover T.L. Extracellular release of antigenic proteins by Helicobacter pylori. Infect. Immun. 1998, 66(6):2984-2986.
    • (1998) Infect. Immun. , vol.66 , Issue.6 , pp. 2984-2986
    • Cao, P.1    McClain, M.S.2    Forsyth, M.H.3    Cover, T.L.4
  • 35
    • 23344448724 scopus 로고    scopus 로고
    • Characterization of the Helicobacter pylori cysteine-rich protein a as a T-helper cell type 1 polarizing agent
    • Deml L., Aigner M., Decker J., Eckhardt A., Schutz C., Mittl P.R., et al. Characterization of the Helicobacter pylori cysteine-rich protein a as a T-helper cell type 1 polarizing agent. Infect. Immun. 2005, 73(8):4732-4742.
    • (2005) Infect. Immun. , vol.73 , Issue.8 , pp. 4732-4742
    • Deml, L.1    Aigner, M.2    Decker, J.3    Eckhardt, A.4    Schutz, C.5    Mittl, P.R.6
  • 36
    • 65549090576 scopus 로고    scopus 로고
    • The secreted helicobacter cysteine-rich protein a causes adherence of human monocytes and differentiation into a macrophage-like phenotype
    • Dumrese C., Slomianka L., Ziegler U., Choi S.S., Kalia A., Fulurija A., et al. The secreted helicobacter cysteine-rich protein a causes adherence of human monocytes and differentiation into a macrophage-like phenotype. FEBS Lett. 2009, 583(10):1637-1643.
    • (2009) FEBS Lett. , vol.583 , Issue.10 , pp. 1637-1643
    • Dumrese, C.1    Slomianka, L.2    Ziegler, U.3    Choi, S.S.4    Kalia, A.5    Fulurija, A.6
  • 37
    • 34548392299 scopus 로고    scopus 로고
    • Helicobacter pylori evolution: lineage- specific adaptations in homologs of eukaryotic Sel1-like genes
    • Ogura M., Perez J.C., Mittl P.R., Lee H.K., Dailide G., Tan S., et al. Helicobacter pylori evolution: lineage- specific adaptations in homologs of eukaryotic Sel1-like genes. PLoS Comput. Biol. 2007, 3(8):e151.
    • (2007) PLoS Comput. Biol. , vol.3 , Issue.8 , pp. e151
    • Ogura, M.1    Perez, J.C.2    Mittl, P.R.3    Lee, H.K.4    Dailide, G.5    Tan, S.6
  • 38
    • 0026758223 scopus 로고
    • Serum neutralizing antibody response to the vacuolating cytotoxin of Helicobacter pylori
    • Cover T.L., Cao P., Murthy U.K., Sipple M.S., Blaser M.J. Serum neutralizing antibody response to the vacuolating cytotoxin of Helicobacter pylori. J. Clin. Invest. 1992, 90(3):913-918.
    • (1992) J. Clin. Invest. , vol.90 , Issue.3 , pp. 913-918
    • Cover, T.L.1    Cao, P.2    Murthy, U.K.3    Sipple, M.S.4    Blaser, M.J.5
  • 39
    • 0037768684 scopus 로고    scopus 로고
    • Detection of high titers of antibody against helicobacter cysteine-rich proteins a, B, C, and E in Helicobacter pylori-infected individuals
    • Mittl P.R., Luthy L., Reinhardt C., Joller H. Detection of high titers of antibody against helicobacter cysteine-rich proteins a, B, C, and E in Helicobacter pylori-infected individuals. Clin. Diagn. Lab. Immunol. 2003, 10(4):542-545.
    • (2003) Clin. Diagn. Lab. Immunol. , vol.10 , Issue.4 , pp. 542-545
    • Mittl, P.R.1    Luthy, L.2    Reinhardt, C.3    Joller, H.4
  • 40
    • 0036205858 scopus 로고    scopus 로고
    • Immunoproteomics of Helicobacter pylori infection and relation to gastric disease
    • Haas G., Karaali G., Ebermayer K., Metzger W.G., Lamer S., Zimny-Arndt U., et al. Immunoproteomics of Helicobacter pylori infection and relation to gastric disease. Proteomics 2002, 2(3):313-324.
    • (2002) Proteomics , vol.2 , Issue.3 , pp. 313-324
    • Haas, G.1    Karaali, G.2    Ebermayer, K.3    Metzger, W.G.4    Lamer, S.5    Zimny-Arndt, U.6
  • 41
    • 0036840999 scopus 로고    scopus 로고
    • A comparison of murine and human immunoproteomes of Helicobacter pylori validates the preclinical murine infection model for antigen screening
    • Bumann D., Holland P., Siejak F., Koesling J., Sabarth N., Lamer S., et al. A comparison of murine and human immunoproteomes of Helicobacter pylori validates the preclinical murine infection model for antigen screening. Infect. Immun. 2002, 70(11):6494-6498.
    • (2002) Infect. Immun. , vol.70 , Issue.11 , pp. 6494-6498
    • Bumann, D.1    Holland, P.2    Siejak, F.3    Koesling, J.4    Sabarth, N.5    Lamer, S.6
  • 43
    • 0036841283 scopus 로고    scopus 로고
    • Multiparameter selection of Helicobacter pylori antigens identifies two novel antigens with high protective efficacy
    • Sabarth N., Hurwitz R., Meyer T.F., Bumann D. Multiparameter selection of Helicobacter pylori antigens identifies two novel antigens with high protective efficacy. Infect. Immun. 2002, 70(11):6499-6503.
    • (2002) Infect. Immun. , vol.70 , Issue.11 , pp. 6499-6503
    • Sabarth, N.1    Hurwitz, R.2    Meyer, T.F.3    Bumann, D.4
  • 44
    • 84893211112 scopus 로고    scopus 로고
    • Oral immunization with recombinant Lactobacillus acidophilus expressing the adhesin Hp0410 of Helicobacter pylori induces mucosal and systemic immune responses
    • Hongying F., Xianbo W., Fang Y., Yang B., Beiguo L. Oral immunization with recombinant Lactobacillus acidophilus expressing the adhesin Hp0410 of Helicobacter pylori induces mucosal and systemic immune responses. Clin. Vaccine Immunol. 2014, 21(2):126-132.
    • (2014) Clin. Vaccine Immunol. , vol.21 , Issue.2 , pp. 126-132
    • Hongying, F.1    Xianbo, W.2    Fang, Y.3    Yang, B.4    Beiguo, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.