Publicado May 17, 2014



PLUMX
Google Scholar
 
Search GoogleScholar
Descargas


Carlos Eduardo Barragán Vidal

Andrés Julián Gutiérrez-Escobar

Lizeth Paola Castiblanco Robayo

##plugins.themes.bootstrap3.article.details##

Resumen

La infección por Helicobacter pylori se relaciona con gastritis, desarrollo de úlceras y cáncer gástrico. Se han dilucidado varios mecanismos fisiopatológicos respecto al proceso de adherencia de este patógeno a las células epiteliales gástricas, de las cuales las proteínas de membrana (PME) constituyen uno de los principales agentes de estudio. El interés por estas proteínas radica no solo en su papel en el proceso de colonización y consecuente desarrollo del proceso patológico, sino también en que algunas de ellas podrían ser consideradas potenciales blancos terapéuticos. En esta revisión se describen las principales PME y su rol en el proceso de adhesión al epitelio, ya que su estudio y caracterización permitirá proponer alternativas eficientes para el control y erradicación de esta infección, que es una de las principales causas asociadas al cáncer gástrico en Colombia y el mundo.

Keywords

Helicobacter pylori, adherence, bacterial outer membrane proteins, pylori, adhesión, proteínas de la membrana bacteriana externa,

References
1. Suerbaum S, Michetti P. Helicobacter pylori infection. N Engl J Med. 2002;347:1175-86.
2. Kusters JG, Vliet AM, Kuipers EJ. Pathogenesis of Helicobacter pylori infection. Clin Microbiol Rev. 2006 July;19(3):449-90.
3. Tomb JF, White O, Kerlavage A et al. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 1997; 388:539–547.
4. Malaty HM. Epidemiology of Helicobacter pylori infection. Best Pract Res Cl Ga. 2007;21(2):205-14.
5. Suzuki H, Hibi T, Marshall BJ. Helicobacter pylori: present status and future prospects in Japan. J Gastroenterol. 2007;42:1-15.
6. Kim SS, Ruiz V, Carroll J, Moss S. Helicobacter pylori in the pathogenesis of gastric cancer and gastric lymphoma. Cancer Lett. 2011;305:228-38.
7. Go MF. Natural history and epidemiology of Helicobacter pylori infection. Aliment Pharmacol Ther. 2002;16(suppl 1):3-15.
8. Thun MJ, DeLancey JO, Center MM, Jemal A, Ward EM. The global burden of cancer: priorities for prevention. Carcinogenesis. 2010;31(1):100-10.
9. Martínez T, Hernández G, Bravo MM et al. Polimorfismos genéticos de interleucinas IL-1B-511, IL-1RN, IL-10, factor
de necrosis tumoral α-308 e infección por Helicobacter pylori CagA positivo en cáncer gástrico y úlcera duodenal en diferentes poblaciones en Colombia. Rev Colomb Canc. 2011;15(2):31-43.
10. Instituto Nacional de Cancerología (INC) de Colombia. Cáncer en cifras: situación actual del cáncer en Colombia. Mortalidad por cáncer según primeras causas y sexo, 2000-2006. 2012 [internet]. [Citado 2014 ene 27]. Disponible en: http://www.cancer.gov.co/documentos/Plandecenalparaelcontroldelcancer/PlanDecenal_ControlCancer_2012-2021.pdf.
11. IARC. IARC monographs of the evaluation of carcinogenic risks to humans. IARC [internet]. 1994 [citado 2014 ene 22];61:177-241. Disponible en: http://monographs.iarc.fr/ENG/Classification/ClassificationsGroupOrder.pdf.
12. Zhang C, Yamada N, Wu YL et al. Helicobacter pylori infection, glandular atrophy and intestinal metaplasia in superficial gastritis, gastric erosion, erosive gastritis, gastric ulcer and early gastric cáncer. World J Gastroenterol. 2005;11:791-6.
13. Amieva MR, Omar EE. Host bacterial interactions in Helicobacter pylori infection. Gastroenterology. 2008;134(1):306-29.
14. Del Giudice G, Michetti P. Inflammation, immunity and vaccines for Helicobacter pylori. Helicobacter. 2004;9(suppl 1):23-8.
15. Wilson KT, Crabtree JE. Immunology of Helicobacter pylori: Insights into the failure of the immune response and perspectives on vaccine studies. Gatroenterology. 2007;133:288-308.
16. O’Keeffe J, Moran AP. Conventional, regulatory, and unconventional T cell in the immunology response to Helicobacter pylori. Helicobacter. 2008;13:1-19.
17. Wessler S, Gimona M, Rieder G. Regulation of the actin cytoskeleton in Helicobacter pylori-induced migration and invasive growth of gastric epithelial cells. Cell Commun Signal. 2011;9(27):1-9.
18. Liechti G, Goldberg J. Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori. Front Cell Infect Microbiol. 2012;2(29):1-18.
19. Fleming SL. Helicobacter pylori. New York: Chelsea House; 2007.
20. Ramírez A, Recavarren S, Arias J et al. Helicobacter pylori, gastritis crónica, úlcera gástrica y úlcera duodenal: estudio de 1638 pacientes. Rev Gastroenterol Perú. 1999;19:196-201.
21. Doig P, Trust TJ. Identification of surface-exposed outer membrane antigens of Helicobacter pylori. Infect Immun. 1994;62:4526-33.
22. Alm R, Bina J, Andrews B et al. Comparative genomics of Helicobacter pylori: analysis of the outer membrane protein families. Infect Immun. 2000;68(7):4155-68.
23. Magalhães A, Reis CA. Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors. Braz J Med Biol Res. 2010;43:611-8.
24. Odenbreit S, Faller G, Haas R. Role of the AlpAB proteins and lipopolysaccharide in adhesion of Helicobacter pylori to human gastric tissue. Int J Med Microbiol. 2002;292(3):247-56.
25. Shao SH, Wang H, Chai SG, Liu LM. Research progress on Helicobacter pylori outer membrane protein. World J Gastroenterol. 2005;11(20):3011-3.
26. Cover T. Role of Helicobacter pylori outer membrane proteins in gastroduodenal disease. J Infect Dis. 2006;194:1343-55.
27. Odenbreit S, Till M, Hofreuter D, Faller G, Haas R. Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue. Mol Microbiol. 1999;31(5):1537-48.
28. Odenbreit S, Swoboda K, Barwig I et al. Outer membrane protein expression profile in Helicobacter pylori clinical isolates. Infect Immun. 2009;77(9):3782-90.
29. Doig P, Exner MM, Hancock RE, Trust TJ. Isolation and characterization of a conserved porin protein from Helicobacter pylori. J Bacteriol. 1995;177(19):5447-52.
30. Evans DG, Evans DJ, Moulds J, Graham D.N-acetylneuraminyllactose-binding fibrillarhemagglutinin of Campylobacter pylori: a putative colonization factor antigen. Infect Immun. 1988;56(11):2896-2906.
31. Evans D, Karjalainen T, Evans D, Graham D, Lee C. Cloning, nucleotide sequence, and expression of a gene encoding an adhesin subunit protein of Helicobacter pylori. J Bacteriol. 1993;175(3):674-83.
32. O’Toole P, Janzon L, Doig P et al. The putative neuraminyllactose-binding hemaglutinin HpaA of Helicobacter pylori CCUG 17874 is a lipoprotein. J Bacteriol. 1995;177(21):6049-57.
33. Carlsohn E, Nystrom J, Bolin I, Nilsson C, Svennerholm A. HpaA is essential for Helicobacter pylori colonization in mice. Infect Immun. 2006;74:920-6.
34. Agudo S. Estudio molecular de los factores de virulencia y de la resistencia a claritromicina en la infección por Helicobacter pylori [internet]. Tesis doctoral, Universidad Complutense de Madrid, España; 2010. Disponible en: http://eprints.ucm.es/11520/1/T32212.pdf
35. Lindholm C, Osek J, Svennerholm A. Quantification of conserved antigens in Helicobacter pylori during different culture conditions. Infect Immun. 1997;65(12):5376-80.
36. Nyström J, Svennerholm A-M. Oral immunization with HpaA affords therapeutic protective immunity against H. pylori that is reflected by specific mucosal immune responses. Vaccine. 2007;25(14):2591-8.
37. Boren T, Falk P, Roth K, Larson G, Normark S. Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science. 1993;262:1892-5.
38. Ilver D, Arnqvist A, Ogren J et al. Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging. Science. 1998;279:373-7.
39. Sheu B, Yang H, Yeh Y, Wu J. Helicobacter pylori colonization of the human gastric epithelium: A bug’s first step is a novel target for us. J Gastroenterol Hepatol. 2010;25:26-32.
40. Torres L, Rodríguez B. Principales factores de patogenia en la infección por Helicobacter pylori. Rev CENIC Cien Biol. 2008;39(1):52-62.
41. Quiroga A, Cittelly D, Bravo MM. Frecuencia de los genotipos BabA2, OipA y CagE de Helicobacter pylori en pacientes colombianos con enfermedades gastroduodenales. Biomédica. 2005;25(3):325-34.
42. Doing P, Jonge B, Alm R et al. Helicobacter pylori physiology predicted from genomic comparison of two strains. Microbiol Mol Biol Rev. 1999;63(3):675-707.
43. Dubreuil J, Giudice G, Rappuoli R. Helicobacter pylori interactions with host serum and extracellular matrix proteins: potential role in the infectious process. Microbiol Mol Biol Rev. 2002;66(4):617-29.
44. Pride D, Blaser M. Concerted evolution between duplicated genetic elements in Helicobacter pylori. J Mol Biol. 2002;316:629-42.
45. Yamaoka Y, Souchek J, Odenbreit S et al. Discrimination between cases of duodenal ulcer and gastritis on the basis of putative virulence factors of Helicobacter pylori. J Clin Microbiol. 2002;40:2244-6.
46. Delahay R, Rugge M. Pathogenesis of Helicobacter pylori infection. Helicobacter. 2012;17(suppl 1):9-15.
47. Olfat F, Zheng Q, Oleastro M et al. Correlation of the Helicobacter pylori adherence factor BabA with duodenal ulcer disease in four European countries. FEMS Immunol Med Microbiol. 2005;44:151-6.
48. Villalobos L. Relación de Helicobacter pylori con la expresión de pepsinógenos, gastrina y respuesta humoral. [internet]. Tesis doctoral, Universidad Simón Bolívar; 2012. Disponible en http://www.dic.coord.usb.ve/Web%20Egresados_archivos/TesisDoctoralVillalobos.pdf
49. Van J, Mahdavi J, Korteland A et al. The MUC5AC glycoprotein is the primary receptor for Helicobacter pylori in the human stomach. Helicobacter. 2003;8(5): 521-32.
50. Yamaoka Y. Roles of Helicobacter pylori BabA in gastroduodenal pathogenesis. World J Gastroenterol. 2008;14:4265-72.
51. Mahdavi J, Sondén B, Hurtig M, et al. Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation. Science. 2002;297(5581):573-8.
52. Yamaoka Y, Ojo O, Fujimoto S et al. Helicobacter pylori outer membrane proteins and gastroduodenal disease. Gut. 2006;55(6):775-81.
53. Unemo M, Aspholm M, Ilver D et al. The sialic acid binding SabA adhesion of Helicobacter pylori essential for nonopsonic activation of human neutrophils. J Biol Chem. 2005;280:15390-7.
54. Odenbreit S. Adherence properties of Helicobacter pylori: impact on pathogenesis and adaptation to the host. Int J Med Microbiol. 2005;295:317-24.
55. Roche N, Angstrom J, Hurtig M et al. Helicobacter pylori and complex gangliosides. Infect Immun. 2004;72:1519-29.
56. Aspholm M, Olfat F, Norden J. SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathog. 2006;2:e110.
57. Yamaoka Y, Kikuch S, el-Zimaity HM et al. Importance of Helicobacter pylori oipA in clinical presentation, gastric inflammation, and mucosal interleukin 8 production. Gastroenterology. 2002; 123(2):414-24.
58. Dossumbekova A, Prinz C, Mages J et al. Helicobacter pylori HopH (OipA) and bacterial pathogenicity: genetic and functional genomic analysis of hopH gene polymorphisms. J Infect Dis. 2006;194(10):1346-55.
59. Markovska R, Boyanova L, Yordanov D, Gergova G, Mitov I. Helicobacter pylori oipA genetic diversity and its associations with both disease and cagA, vacA s, m, and i alleles among Bulgarian patients. Diagn Microbiol Infect Dis. 2011;71(4):335-40.
60. Senkovich O, Yin J, Ekshyyan V et al. Helicobacter pylori AlpA and AlpB bind host laminin and influence gastric inflammation in gerbils. Infec Immun. 2011;79(8):3106-16.
61. Kim N, Weeks D, Moo J et al. Proteins released by Helicobacter pylori in vitro. J Bacteriol. 2002;184(22):6155-62.
62. Jonge R, Durrani Z, Rijpkema S et al. Role of the Helicobacter pylori outermembrane proteins AlpA and AlpB in colonization of the guinea pig stomach. J Med Microbiol. 2004;53:375-9.
63. Lu H, Wu J, Beswick E et al. Functional and intracellular signaling differences associated with the Helicobacter pylori AlpAB adhesin from western and East Asian strains. J Biol Chem. 2007;282(9):6242-54.
64. Xue J, Bai Y, Chen Y et al. Expression of Helicobacter pylori AlpA protein and its immunogenicity. World J Gastroenterol. 2005;11(15):2260-3.
65. Snelling WJ, Moran AP, Ryan KA et al. HorB (HP0127) is a gastric epithelial cell adhesin. Helicobacter. 2007;12(3):200-9.
66. Taghvaei T, Abadi A, Ghasemzadeh A, Naderi BK, Mobarez AM. Prevalence of horB gene among the Helicobacter pylori strains isolated from dyspeptic patients: first report from Iran. Int Emerg Med. 2012;7(6):505-8.
67. Edwards NJ, Monteiro MA, Faller G et al. Lewis X structures in the O antigen sidechain promote adhesion of Helicobacter pylori to the gastric epithelium. Mol Microbiol. 2000;35(6):1530-9.
68. Mahdavi J, Bore´n T, Vandenbroucke C, Appelmelk B. Limited role of lipopolysaccharide Lewis antigens in adherence of Helicobacter pylori to the human gastric epithelium. Infect Immun. 2003;71 (5):2876-80.
69. Bina J, Bains M, Hancock RE. Functional expression in Escherichia coli and membrane topology of porin HopE, a member of a large family of conserved proteins in Helicobacter pylori. J Bacteriol. 2000;182(9):2370-5.
70. Bernarde C, Lehours P, Lasserre JP et al. Complexomics study of two Helicobacter pylori strains of two pathological origins. Potential targets for vaccine development and new insight in bacteria metabolism. Mol Cell Proteom. 2010;9(12):2796-2826.
71. Cao P, Lee KJ, Blaser MJ, Cover TL. Analysis of hopQ alleles in East Asian and western strains of Helicobacter pylori. FEMS Microbiol Lett. 2005;251(1):37-43.
72. Loh JT, Torres VJ, Scott Algood HM, McClain MS, Cover TL. Helicobacter pylori HopQ outer membrane protein attenuates bacterial adherence to gastric epithelial cells. FEMS Microbiol Lett. 2008;289(1):53-8.
73. Moran AP. Lipopolysaccharide in bacterial chronic infection: insights from Helicobacter pylori lipopolysaccharide and lipid A. Int J Med Microbiol. 2007; 297(5):307-19.
74. Fischer W. Assembly and molecular mode of action of the Helicobacter pylori Cag type IV secretion apparatus. FEBS J. 2011;278(8):1203-12.
75. Acosta P, Delgado M, Montealegre M, Echeverry M, Henao C. Caracterización molecular y bioinformática de la proteína CagA de Helicobacter pylori a partir de biopsias gástricas de pacientes colombianos. Rev Colomb Gastroenterol. 2009;24(4):353-62.
76. Furuta Y, Yahara K, Hatakeyama M, Kobayashi I. Evolution of cagA oncogene of Helicobacter pylori through recombination. PLoS ONE. 2011;6(23499):1-11.
77. Peek R, Fiske C, Wilson K. Role or innate immunity in Helicobacter pyloriinduced gastric malignancy. Physiol Rev. 2010;90:831-58.
78. Saha A, Backert S, Hammond CE, Gooz M, Smolka AJ. Helicobacter pylori CagL activates ADAM17 to induce repression of the gastric H, K-ATPase α subunit. Gastroenterology. 2010;139(1):239-48.
79. Witkowska D, Rowinska-Zyrek M, Valensin G, Kozlowski H. Specific polyhistidyl and poly-cysteil protein sites involved in Ni2+ homeostasis in Helicobacter pylori. Impact of Bi3+ ions on Ni2+ binding to proteins. Structural and thermodynamic aspects. Coord Chem Rev. 2012;256(1):133-48.
80. Davis GS, Flannery EL, Mobley HL. Helicobacter pylori HP1512 is a nickelresponsive NikR-regulated outer membrane protein. Infect Immun. 2006; 74(12):6811-20.
81. Ernst F, Bereswill S, Waidner B et al. Transcriptional profiling of Helicobacter pylori Fur-and iron-regulated gene expression. Microbiology. 2005;151:533-46.
82. Miles S, Piazuelo M, Mora C et al. Detailed in vivo analysis of the role of Helicobacter pylori Fur in colonization and disease. Infect Immun. 2010;78(7):3073-82.
83. Tsugawa H, Suzuki H, Matsuzaki J, Hirata K, Hibi T. FecA1, a bacterial iron transporter, determines the survival of Helicobacter pylori in the stomach. Free Radic Biol Med. 2012;52(6):1003-10.
84. Spohn G, Scarlato V. Motility, chemotaxis, and flagella. En: Mobley HLT, Mendz GL, Hazell SL, editores. Helicobacter pylori: Physiology and genetics [internet]. Washington (DC): ASM Press; 2001. Disponible en http://www.ncbi.nlm.nih.gov/books/NBK2423/.
85. Joseph I, Kirschner D. A model for the study of Helicobacter pylori interaction with human gastric acid secretion. J Theor Biol. 2004;228(1):55-80.
86. Kikuchi K, Murata-Kamiya N, Kondo S, Hatakeyama M. Helicobacter pylori stimulates epithelial cell migration via CagA-mediated perturbation of host cell signaling. Microb Infect. 2012;14(5):470-476.
87. Machado A, Figueiredo, Seruca R, Rasmussen L. Helicobacter pylori infection generates genetic instability in gastric cells. Biochem Biophys Acta. Reviews on Cancer. 2010;1806:58-65.
88. Backert S, Selbach M. Role of type IV secretion in Helicobacter pylori pathogenesis. Cell Microbiol. 2008; 10(8):1573-81.89. Müller A, Oertli M, Arnold I. H. pylori exploits and manipulates innate and adaptive immune cell signaling pathways to establish persistent infection. Cell Comm Signal. 2011;9(25):1-9.
90. Portal C, Pérez G. Immune responses to Helicobacter pylori colonization: mechanisms and clinical outcomes. Clin Sci. 2006;110:305-14.
91. Galvis A. Prevalencia de los genotipos de virulencia de Helicobacter pylori CagA, VacA, babA2 e IceA en pacientes colombianos con dispepsia funcional [internet]. Trabajo de grado, Magíster en Ciencias Biológicas, Pontificia Universidad Javeriana, Colombia; 2010. Disponible en http://repository.javeriana.edu.co/bitstream/10554/818/1/cien20.pdf
92. Shiota S, Watada M, Matsunari O et al. Helicobacter pylori iceA, clinical outcomes, and correlation with cagA: a meta-analysis. PloS One. 2012;7(1):e30354.
93. Yamaoka Y, Kodama T, Gutierrez O et al. Relationship between Helicobacter pylori IceA, CagA, and VacA status and clinical outcome: studies in four different countries. J Clin Microbiol. 1999;37(7):2274-9.
94. Ming K, Leong T. Epidemiology of Helicobacter pylori infection and gastric cancer in Asia. J Gastroenterol Hepatol. 2010;25(3):479-86.
95. Gutiérrez-Escobar A. Análisis evolutivo de la adhesión: evidencia de selección positiva operante sobre el locus AlpAB y el gen horB de Helicobacter pylori. Revista UDCA. 2013;16(1):3-15.
Cómo citar
Barragán Vidal, C. E., Gutiérrez-Escobar, A. J., & Castiblanco Robayo, L. P. (2014). Membrana externa de Helicobacter pylori y su papel en la adhesión al epitelio gástrico. Universitas Medica, 56(1), 44-62. Recuperado a partir de https://revistas.javeriana.edu.co/index.php/vnimedica/article/view/16344
Sección
Artículos de revisión