Asian Pacific Journal of Cancer Prevention

  • 제14권3호
  • /
  • Pages.1635-1642
  • /
  • 2013
  • /
  • 1513-7368(pISSN)
  • /
  • 2476-762X(eISSN)
아시아태평양암예방학회 (Asian Pacific Journal of Cancer Prevention)
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Antigenic Proteins of Helicobacter pylori of Potential Diagnostic Value

  • Khalilpour, Akbar (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Santhanam, Amutha (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Lee, Chun Wei (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Saadatnia, Geita (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Velusamy, Nagarajan (Hospital Seberang Jaya) ;
  • Osman, Sabariah (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Mohamad, Ahmad Munir (Institute for Research in Molecular Medicine, Universiti Sains Malaysia) ;
  • Noordin, Rahmah (Institute for Research in Molecular Medicine, Universiti Sains Malaysia)
  • 발행 : 2013.03.30
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초록

Helicobacter pylori antigen was prepared from an isolate from a patient with a duodenal ulcer. Serum samples were obtained from culture-positive H. pylori infected patients with duodenal ulcers, gastric ulcers and gastritis (n=30). As controls, three kinds of sera without detectable H. pylori IgG antibodies were used: 30 from healthy individuals without history of gastric disorders, 30 from patients who were seen in the endoscopy clinic but were H. pylori culture negative and 30 from people with other diseases. OFF-GEL electrophoresis, SDS-PAGE and Western blots of individual serum samples were used to identify protein bands with good sensitivity and specificity when probed with the above sera and HRP-conjugated anti-human IgG. Four H. pylori protein bands showed good (${\geq}$ 70%) sensitivity and high specificity (98-100%) towards anti-Helicobacter IgG antibody in culture-positive patients sera and control sera, respectively. The identities of the antigenic proteins were elucidated by mass spectrometry. The relative molecular weights and the identities of the proteins, based on MALDI TOF/TOF, were as follows: CagI (25 kDa), urease G accessory protein (25 kDa), UreB (63 kDa) and proline/pyrroline-5-carboxylate dehydrogenase (118 KDa). These identified proteins, singly and/or in combinations, may be useful for diagnosis of H. pylori infection in patients.

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참고문헌

  1. Andersen LP, Espersen F (1992). Immunoglobulin G antibodies to Helicobacter pylori in patients with dyspeptic symptoms investigated by the western immunoblot technique. J Clin Microbiol, 30, 1743-51.
  2. Alam J, Maiti S, Ghosh P, et al (2012). Significant association of the dupA gene of Helicobacter pylori with duodenal ulcer development in a South-east Indian population. J Med Microbiol, 61, 1295-302. https://doi.org/10.1099/jmm.0.038398-0
  3. Baik SC, Kim KM, Song SM, et al (2004). Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Helicobacter pylori strain 26695. J Bacteriol, 186, 949-55. https://doi.org/10.1128/JB.186.4.949-955.2004
  4. Benoit S, Mehta N, Wang G, Gatlin M, Maier RJ (2004). Requirement of hydD, hydE, hypC and hypE genes for hydrogenase activity in Helicobacter pylori. Microb Pathog, 36, 153-7. https://doi.org/10.1016/j.micpath.2003.11.001
  5. Bergey B MP, Peacock J, Megraud F (2003). What is the role of serology in assessing Helicobacter pylori eradication. Alimentary pharmacology & therapeutics, 18, 635-9. https://doi.org/10.1046/j.1365-2036.2003.01716.x
  6. Besra GS, Kremer L, Nampoothiri KM, et al (2001). Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA: AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J Biological Chemistry, 76, 27967-74.
  7. Chan CH, Ko CC, Chang JG, et al (2006). Subcellular and functional proteomic analysis of the cellular responses induced by Helicobacter pylori. Mol Cell Proteomics, 4, 702-13.
  8. Chambers MG, Pyburn TM, et al (2013). Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin. J Mol Biol, 425, 524-35. https://doi.org/10.1016/j.jmb.2012.11.020
  9. Chisholm SA, Owen RJ (2008). Application of polymerase chain reaction-based assays for rapid identification and antibiotic resistance screening of Helicobacter pylori in gastric biopsies. Diagn Microbiol Infect Dis, 61, 67-71. https://doi.org/10.1016/j.diagmicrobio.2007.12.005
  10. Chomvarin C, Ottiwet O, Hahnvajanawong C, Intapan PM, Wongwajana S (2009). Seroreactivity to specific antigens of Helicobacter pylori infection is associated with an increased risk of the dyspeptic gastrointestinal diseases. Int J Infect Dis, 13, 647-54. https://doi.org/10.1016/j.ijid.2008.12.013
  11. Crabtree JE, Shallcross TM, Heatley RV, Wyatt JI (1991). Evaluation of a commercial ELISA for serodiagnosis of Helicobacter pylori infection. J Clin Pathology, 44, 326-8. https://doi.org/10.1136/jcp.44.4.326
  12. Cremonini F, Gabrielli M, Gasbarrini G, Pola P, Gasbarrini A (2004). The relationship between chronic H. pylori infection, CagA seropositivity and stroke: meta-analysis. Atherosclerosis, 173, 253-9. https://doi.org/10.1016/j.atherosclerosis.2003.12.012
  13. Evans DJJ, Evans DG, Graham DY, Klein PD (1989). A sensitive and specific serologic test for detection of Campylobacter pylori infection. Gastroenterology, 96, 1004-8.
  14. Flores-luna L, Camorlinga-Ponce M, Hernendez-Suarez G, et al (2013). The utility of serologic tests as biomarkers for Helicobacter pylori-associated precancerous lesions and gastric cancer varies between Latin American countries. Cancer Causes Control, 24, 241-8. https://doi.org/10.1007/s10552-012-0106-8
  15. Faulde M, Putzker M, Mertes T, Sobe D (1991). Evaluation of an immunofluorescence assay for specific detection of immunoglobulin G antibodies directed against Helicobacter pylori, and antigenic cross-reactivity between H. pylori and Campylobacter jejuni. J Clin Microbiol, 29, 323-7.
  16. Franceschi F, Gasbarrini A (2007). Helicobacter pylori and extragastric diseases. Best Pract Res Clin Gastroenterol, 21, 325-34. https://doi.org/10.1016/j.bpg.2006.10.003
  17. Galmiche A, Rassow J, Doye A, et al (2000). The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release. EMBO J, 19, 6361-70. https://doi.org/10.1093/emboj/19.23.6361
  18. Ge R, Sun X, Gu Q, et al (2007). A proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori. J Biol Inorg Chem, 12, 831-42. https://doi.org/10.1007/s00775-007-0237-7
  19. Giannakis M, Chen SL, Karam SM, Engstrand L, Gordon JI (2008). Helicobacter pylori evolution during progression from chronic atrophic gastritis to gastric cancer and its impact on gastric stem cells. Proc Natl Acad Sci USA, 105, 4358-63. https://doi.org/10.1073/pnas.0800668105
  20. Glassman MS, Dallal S, Berezin SH, et al (1990). Helicobacter pylori-related gastroduodenal disease in children. Diagnostic utility of enzyme-linked immunosorbent assay. Dig Dis Sci, 35, 993-7. https://doi.org/10.1007/BF01537248
  21. Graham DY, Evans DJ, Jr, Peacock J, Baker JT, Schrier WH (1996). Comparison of rapid serological tests (FlexSure HP and QuickVue) with conventional ELISA for detection of Helicobacter pylori infection. Am J Gastroenterology, 91, 942-8.
  22. Haas G, Karaali G, Ebermayer K, et al (2002). Immunoproteomics of Helicobacter pylori infection and relation to gastric disease. Proteomics, 2, 313-24. https://doi.org/10.1002/1615-9861(200203)2:3<313::AID-PROT313>3.0.CO;2-7
  23. Hambers MG, Pyburn TM, Gonzalez-rivera C, et al (2013). Structural analysis of the oligomeric states of Helicobacter pylori VacA toxin. J Mol Biol, 425, 524-35. https://doi.org/10.1016/j.jmb.2012.11.020
  24. Inagaki E, Ohshima N, Takahashi H, et al (2006). Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase. J Mol Biol, 362, 490-501. https://doi.org/10.1016/j.jmb.2006.07.048
  25. Jensen AKV, Andersen LP, Gaarslev K, Wachmann CH (1993). Comparison of four second generation kits for detection of IgG antibodies against Helicobacter pylori in adults. Zentralblatt fur Bakteriologie, 280, 221-6. https://doi.org/10.1016/S0934-8840(11)80959-X
  26. Jimenez-Soto LF KS, Sewald X, Ertl C, et al (2009). Helicobacter pylori type IVsecretion apparatus exploits b1 integrin in anovel RGD-independent manner. PLoS Pathog, 5,1000684. https://doi.org/10.1371/journal.ppat.1000684
  27. Jungblut PR, Bumann D, Haas G, et al (2000). Comparative proteome analysis of Helicobacter pylori. Mol Microbiol, 36,710-25.
  28. Keenan J OJ, Domigan N, Potter H, et al (2000). Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate. Infect Immun, 68, 3337-43. https://doi.org/10.1128/IAI.68.6.3337-3343.2000
  29. Keenan J, Oliaro J, Domigan N, et al (2000). Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate. Infect Immun, 68, 3337-43. https://doi.org/10.1128/IAI.68.6.3337-3343.2000
  30. Khanna B, Cutler A, Israel NR, et al (1998). Use caution with serologic testing for Helicobacter pylori infection in children. J Infectious Diseases, 178, 460-5. https://doi.org/10.1086/515634
  31. Krah A, Miehlke S, Pleissner KP, et al (2004). Identification of candidate antigens for serologic detection of Helicobacter pylori-infected patients with gastric carcinoma. Int J Cancer, 108, 456-63. https://doi.org/10.1002/ijc.11557
  32. Krah A MS, Pleissner KP, Zimny-Arndt U, et al (2004). Identification of candidate antigens for serologic detection of Helicobacter pylori-infected patients with gastric carcinoma. Int J Cancer, 108, 456-63. https://doi.org/10.1002/ijc.11557
  33. Kwok T, Zabler D, Urman S, et al (2007). Helicobacter exploits integrin for type IV secretion and kinase activation. Nature, 449, 862-6. https://doi.org/10.1038/nature06187
  34. Leung WK, Ng EKW, Chan FKL, Chung SCS, Sung JJY (1999). Evaluation of three commercial enzyme-linked immunosorbent assay kits for diagnosis of Helicobacter pylori in Chinese patients. Diagnostic Microbiology and Infectious Disease, 34, 13-17. https://doi.org/10.1016/S0732-8893(99)00002-4
  35. Lin Y-F, Chen C-Y, Tsai M-H, et al (2007). Duodenal ulcerrelated antigens from Helicobacter pylori. Immunoproteome and protein microarray approaches. Molecular and Cellular Proteomics, 6, 1018-26. https://doi.org/10.1074/mcp.M700009-MCP200
  36. Lochhead P, El-Omar EM (2007). Helicobacter pylori infection and gastric cancer. Best Pract Res Clin Gastroenterol, 21, 281-97. https://doi.org/10.1016/j.bpg.2007.02.002
  37. Malaty HM (2007). Epidemiology of Helicobacter pylori infection. Best Pract Res Clin Gastroenterol, 21, 205-14.
  38. Manes G BA, Iaquinto G, Ricci C, et al (2001). Accuracy of the stool antigen test in the diagnosis of Helicobacter pylori infection before treatment and in patients on omeprazole therapy. Aliment Pharmacol Ther, 15, 73-9. https://doi.org/10.1046/j.1365-2036.2001.00907.x
  39. Manes G, Balzano A, Iaquinto G, et al (2001). Accuracy of stool antigen test in posteradication assessment of Helicobacter pylori infection. Dig Dis Sci, 46, 2440-4. https://doi.org/10.1023/A:1012319718848
  40. Manes G, Zanetti MV, Piccirillo MM, et al (2005). Accuracy of a new monoclonal stool antigen test in post-eradication assessment of Helicobacter pylori infection: comparison with the polyclonal stool antigen test and urea breath test. Dig Liver Dis, 37, 751-5. https://doi.org/10.1016/j.dld.2005.03.012
  41. Mao YF, Yan J (2004). Construction of prokaryotic expression system of ureB gene from a clinical Helicobacter pylori strain and identification of the recombinant protein immunity. World J Gastroenterology, 10, 977-84.
  42. Marchildon PA, Ciota LM, Zamaniyan FZ, Peacock JS, Graham DY (1996). Evaluation of three commercial enzyme immunoassays compared with the 13C urea breath test for detection of Helicobacter pylori infection. J Clin Microbiology, 34, 1147-52.
  43. Meijer BC, Thijs JC, Kleibeuker JH, van Zwet AA, Berrelkamp RJP (1997). Evaluation of eight enzyme immunoassays for detection of immunogloblin G against Helicobacter pylori. J Clinical Microbiology, 35, 292-4.
  44. Michetti P KC, Kotoff K, Porta N, et al (1999). Oral immunization with urease and Escherichia coli heat-labile enterotoxin is safe and immunogenic in Helicobacter pyloriinfected adults. Gastroenterology, 116, 804-12. https://doi.org/10.1016/S0016-5085(99)70063-6
  45. Mini R, Bernardini G, Salzano AM, et al (2006). Comparative proteomics and immunoproteomics of Helicobacter pylori related to different gastric pathologies. J Chromatography B, Analytical Technologies in the Biomedical and Life Sciences, 833, 63-79. https://doi.org/10.1016/j.jchromb.2005.12.052
  46. Miwa H, Go MF, Sato N (2002). H. pylori and gastric cancer: the Asian enigma. Am J Gastroenterol, 97, 1106-12. https://doi.org/10.1111/j.1572-0241.2002.05663.x
  47. Miwa H, Akamatsu S, Tachikawa T, et al (2001). On-site diagnosis of H. pylori infection by urine. Diagn Microbiol Infect Dis, 39, 95-7. https://doi.org/10.1016/S0732-8893(01)00205-X
  48. Miwa H, Kikuchi S, Ohtaka K, et al (2000). Insufficient diagnostic accuracy of imported serological kits for Helicobacter pylori infection in Japanese population. Diagnostic Microbiology Infectious Disease, 36, 95-9. https://doi.org/10.1016/S0732-8893(99)00143-1
  49. Mobley HL (1996). The role of Helicobacter pylori urease in the pathogenesis of gastritis and peptic ulceration. Aliment Pharmacol Ther, 10, 157-64. https://doi.org/10.1046/j.1365-2036.1996.723115000.x
  50. Noto JM, Gaddy JA, Lee JY, et al (2013). Iron deficiency accelerates Helicobacter pylori-induced carcinogenesis in rodents and humans. J Clin Invest, 123, 479-92. https://doi.org/10.1172/JCI64373
  51. O'Connell KL, Stalts JT (1997). Identification of mouse liver proteins on two-dimensional electrophoresis gel by matrixassociated larser desorption/ ionization mass spectrometry of in situ enzymatic digests. Electrophoresis, 18, 349-59. https://doi.org/10.1002/elps.1150180309
  52. Obata Y, Kikuchi S, Miwa H, et al (2003). Diagnostic accuracy of serological kits for Helicobacter pylori infection with the same assay system but different antigens in a Japanese patient population. J Medical Microbiology, 52, 889-92. https://doi.org/10.1099/jmm.0.05267-0
  53. Ohtsuka Y, Shimada T, Watanabe N, et al (1997). Analysis of the vacA gene sequences among Helicobacter pylori strains isolated from Japanese patients. Gastroenterology, 112, 243.
  54. Park J-W, Song J-Y, Lee S-G, et al (2006). Quantitative analysis of representative proteome components and clustering of Helicobacter pylori clinical strains. Helicobacter, 11, 533-43. https://doi.org/10.1111/j.1523-5378.2006.00456.x
  55. Parsons TB, Ghellamallah C, Male L, Spencer N, Grainger RS (2011). Regioselective dibromination of methyl indole-3-carboxylate and application in the synthesis of 5,6-dibromoindoles. Org Biomol Chem, 9, 5021-3. https://doi.org/10.1039/c1ob05522d
  56. Pelerito A, Oleastro M, Lopes AI, et al (2006). Evaluation of rapid test Assure Helicobacter pylori for diagnosis of H. pylori in pediatric population. J Microbiol Methods, 66, 331-5. https://doi.org/10.1016/j.mimet.2005.12.013
  57. Rieder G, Fischer W, Haas R (2005). Interaction of Helicobacter pylori with host cells: function of secreted and translocated molecules. Curr Opin Microbiol, 8, 67-73. https://doi.org/10.1016/j.mib.2004.12.004
  58. Robinson K, Argent RH, Atherton JC (2007). The inflammatory and immune response to Helicobacter pylori infection. Best Pract Res Clin Gastroenterol, 21, 237-59. https://doi.org/10.1016/j.bpg.2007.01.001
  59. Sasidharan S, Uyub AM (2009). Antibody response to Helicobacter pylori excretory antigen and the cross reaction study. J Immunoassay Immunochem, 30, 70-81.
  60. Schumann C, Triantafilou K, Rasche FM, et al (2006). Serum antibody positivity for distinct Helicobacter pylori antigens in benign and malignant gastroduodenal disease. IJMM, 296, 223-8.
  61. Shevchenko A, Wilm M, Vorm O, Mann M (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem, 68, 850-8. https://doi.org/10.1021/ac950914h
  62. Simor AE, Lin E, Saibil F, et al (1996). Evaluation of enzyme immunoassay for detection of salivary antibody to Helicobacter pylori. J Clin Microbiol, 34, 550-3
  63. Tay Y, Mitchell H, Dong Q, et al (2009). Population structure of Helicobacter pylori among ethnic groups in Malaysia: recent acquisition of the bacterium by the Malay population. BMC Microbiology, 9, 1-13. https://doi.org/10.1186/1471-2180-9-1
  64. Torres J, Camorlinga-Ponce M, Perez-Perez G, Munoz L, Munoz O (2002). Specific serum immunoglobulin G response to urease and CagA antigens of Helicobacter pylori in infected children and adults in a country with high prevalence of infection. Clin Diagn Lab Immunol, 9, 97-100.
  65. Utt M, Nilsson I, Ljungh A, Wadstrom T (2002). Identification of novel immunogenic proteins of Helicobacter pylori by proteome technology. J Immunological Methods, 259, 1-10. https://doi.org/10.1016/S0022-1759(01)00476-8
  66. Vaira D, Vakil N (2001). Blood, urine, stool, breath, money, and Helicobacter pylori. Gut, 48, 287-9. https://doi.org/10.1136/gut.48.3.287
  67. Voland P, Weeks DL, Vaira D, Prinz C, Sachs G (2002). Specific identification of three low molecular weight membraneassociated antigens of Helicobacter pylori. Alimentary Pharmacology & Therapeutics, 16, 533-44. https://doi.org/10.1046/j.1365-2036.2002.01221.x
  68. Widmer M, de Korwin JD, Aucher P, et al (1999). Performance of native and recombinant antigens for diagnosis of Helicobacter pylori infection. Eur J Clin Microbiol Infect Dis, 18, 823-6. https://doi.org/10.1007/s100960050409
  69. Wu M-S, Chow L-P, Lin J-T, Chiou S-H (2008). Proteomic identification of biomarkers related to Helicobacter pylori-associated gastroduodenal disease: challenges and opportunities. J Gastroenterol Hepatol, 23, 1657-61. https://doi.org/10.1111/j.1440-1746.2008.05659.x
  70. Zhang C, Xu S, Xu D (2012). Risk assessment of gastric cancer caused by Helicobacter pylori using CagA sequence markers. PLoS One, 7, 36844. https://doi.org/10.1371/journal.pone.0036844
  71. Zhang X, Shen W, Lu Y, et al (2010). Expression of UreB and HspA of Helicobacter pylori in silkworm pupae and identification of its immunogenicity. Mol Biol Rep, 38, 3173-80.
  72. Zambelli B, Turano P, Musiani F, Neyroz P, Ciurli S (2009). Zn2+-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation. Proteins: Structure, Function, and Bioinformatics, 74, 222-39.
  73. Zheng J, Xiao- Hong T, Huang A-L, Wang P-L (2002). A study of recombinant Protective H. pylori antigens. World J Gastroenterology, 8, 308-11.

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