Abstract
Helicobacter pylori is remarkably adapted to survival in its niche on the surface of the human gastric mucosa. It persists for decades with minimal damage in the majority of those infected. Nevertheless, infection is almost invariably associated with some degree of chronic active gastritis. The intensity of this inflammation of the gastric mucosa has been correlated with the risk of developing complications of the infection such as peptic ulcer, and the inflammation invariably abates after successful elimination of the infection. To modulate the host response, H. pylori has evolved a complex set of genes. Recent genetic studies contributed to defining the function of some of these genes. In addition, these studies, as well as the analysis of the two complete genomes of H. pylori, have provided important information regarding the mechanisms by which H. pylori modulates gene expression. Gene regulation allows the pathogen to further adapt to its environment and to further modulate its relationship to its host, including inflammation.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Segal ED, Falkow S, Tompkins LS. Helicobacter pylori attachment to gastric cells induces cytoskeletal rearrangements and tyrosine phosphorylation of host cell proteins. Proc Natl Acad Sci USA. 1996;93:1259–1264.
Keates S, Hitti YS, Upton M, Kelly CP. Helicobacter pylori infection activates NF-kappa B in gastric epithelial cells. Gastroenterology. 1997;113:1099–1109.
Iiver D, Arnqvist A, Ogren J et al. Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging. Science. 1998;279:373–377.
Guruge JL, Falk PG, Lorenz RG et al. Epithelial attachment alters the outcome of Helicobacter pylori infection. Proc Natl Acad Sci USA. 1998;95:3925–3930.
Gerhard M, Lehn N, Neumayer N et al. Clinical relevance of the Helicobacter pylori gene for blood-group antigen-binding adhesin. Proc Natl Acad Sci USA. 1999;96:12778–12783.
Syder AJ, Guruge JL, Li Q et al. Helicobacter pylori attaches to NeuAc alpha 2,3Gal beta 1,4 glycoconjugates produced in the stomach of transgenic mice lacking parietal cells. Mol Cell. 1999;3:263–274.
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;31:1537–1548.
Cunningham MD, Seachord C, Ratcliffe K, Bainbridge B, Aruffo A, Darveau RP. Helicobacter pylori and Porphyromonas gingivalis lipopolysaccharides are poorly transferred to recombinant soluble CD14. Infect Immun. 1996;64:3601–3608.
Kirkland T, Viriyakosol S, Perez-Perez GI, Blaser MJ. Helicobacter pylori lipopolysaccha-ride can activate 70Z/3 cells via CD14. Infect Immun. 1997;65:604–608.
Semeraro N, Montemurro P, Piccoli C et al. Effect of Helicobacter pylori lipopolysaccharide (LPS) and LPS derivatives on the production of tissue factor and plasminogen activator inhibitor type 2 by human blood mononuclear cells. J Infect Dis. 1996;174:1255–1260.
Sakagami T, Vella J, Dixon MF et al. The endotoxin of Helicobacter pylori is a modulator of host-dependent gastritis. Infect Immun. 1997;65:3310–3316.
Wirth HP, Yang M, Peek RM, Jr, Tham KT, Blaser MJ. Helicobacter pylori Lewis expression is related to the host Lewis phenotype. Gastroenterology. 1997;113:1091–1098.
de Figueiredo Soares T, de Magalhaes Queiroz DM, Mendes EN et al. The interrelationship between Helicobacter pylori vacuolating cytotoxin and gastric carcinoma. Am J Gastroenterol. 1998;93:1841–1847.
Rudi J, Kolb C, Maiwald M et al. Diversity of Helicobacter pylori vacA and cagA genes and relationship to VacA and CagA protein expression, cytotoxin production, and associated diseases (see comments). J Clin Microbiol. 1998;36:944–948.
Yang JC, Kuo CH, Wang HJ, Wang TC, Chang CS, Wang WC. Vacuolating toxin gene polymorphism among Helicobacter pylori clinical isolates and its association with ml, m2, or chimeric vacA middle types. Scand J Gastroenterol. 1998;33:1152–1157.
Miehlke S, Meining A, Morgner A et al. Frequency of vacA genotypes and cytotoxin activity in Helicobacter pylori associated with low-grade gastric mucosa-associated lymphoid tissue lymphoma. J Clin Microbiol. 1998;36:2369–2370.
Yamaoka Y, Kodama T, Kita M, Imanishi J, Kashima K, Graham DY. Relationship of vacA genotypes of Helicobacter pylori to cagA status, cytotoxin production, and clinical outcome. Helicobacter. 1998;3:241–243.
Pagliaccia C, de Bernard M, Lupetti P et al. The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating activity. Proc Natl Acad Sci USA. 1998;95:10212–10217.
Massari P, Manetti R, Burroni D et al. Binding of the Helicobacter pylori vacuolating cytotoxin to target cells. Infect Immun. 1998;66:3981–3984.
Sommi P, Ricci V, Fiocca R et al. Persistence of Helicobacter pylori VacA toxin and vacuolating potential in cultured gastric epithelial cells. Am J Physiol. 1998;275:G681–868.
de Bernard M, Burroni D, Papini E, Rappuoli R, Telford J, Montecucco C. Identification of the Helicobacter pylori VacA toxin domain active in the cell cytosol. Infect Immun. 1998;66:6014–6016.
Pai R, Wyle FA, Cover TL, Itani RM, Domek MJ, Tarnawski AS. Helicobacter pylori culture supernatant interferes with epidermal growth factor-activated signal transduction in human gastric KATO III cells. Am J Pathol. 1998;152:1617–1624.
Papini E, Satin B, Norais N et al. Selective increase of the permeability of polarized epithelial cell monolayers by Helicobacter pylori vacuolating toxin. J Clin Invest. 1998;102:813–820.
Molinari M, Salio M, Galli C et al. Selective inhibition of Ii-dependent antigen presentation by Helicobacter pylori toxin VacA. J Exp Med. 1998;187:135–140.
Sutton P, Wilson J, Genta R et al. A genetic basis for atrophy: dominant non-responsiveness and Helicobacter induced gastritis in F(l) hybrid mice (See comments). Gut. 1999;45:335–340.
Wirth HP, Beins MH, Yang M, Tham KT, Blaser MJ. Experimental infection of Mongolian gerbils with wild-type and mutant Helicobacter pylori strains. Infect Immun. 1998;66:4856–4866.
Gunn MC, Stephens JC, Stewart JA, Rathbone BJ, West KP. The significance of cagA and vacA subtypes of Helicobacter pylori in the pathogenesis of inflammation and peptic ulceration. J Clin Pathol. 1998;51:761–764.
Glocker E, Lange C, Covacci A, Bereswill S, Kist M, Pahl HL. Proteins encoded by the cag pathogenicity island of Helicobacter pylori are required for NF-kappaB activation. Infect Immun. 1998;66:2346–2348.
Akopyants NS, Clifton SW, Kersulyte D et al. Analyses of the cag pathogenicity island of Helicobacter pylori. Mol Microbiol. 1998;28:37–53.
Crabtree JE, Kersulyte D, Li SD, Lindley IJ, Berg DE. Modulation of Helicobacter pylori induced interleukin-8 synthesis in gastric epithelial cells mediated by cag PAI encoded VirD4 homologue. J Clin Pathol. 1999;52:653–657.
Odenbreit S, Puls J, Sedlmaier B, Gerland E, Fischer W, Haas R. Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion. Science. 2000;287:1497–1500.
Segal ED, Cha J, Lo J, Falkow S, Tompkins LS. Altered states: involvement of phosphorylated CagA in the induction of host cellular growth changes by Helicobacter pylori. Proc Natl Acad Sci USA. 1999;96:14559–14564.
Peek RM Jr, Thompson SA, Donahue JP et al. Adherence to gastric epithelial cells induces expression of a Helicobacter pylori gene, iceA, that is associated with clinical outcome. Proc Assoc Am Phys. 1998;110:531–544.
Nishiya D, Shimoyama T, Fukuda S, Yoshimura T, Tanaka M, Munakata A. Evaluation of the clinical relevance of the iceA1 gene in patients with Helicobacter pylori infection in Japan. Scand J Gastroenterol. 2000;35:36–39.
van Doom LJ, Figueiredo C, Sanna R et al. Clinical relevance of the cagA, vacA, and iceA status of Helicobacter pylori. Gastroenterology. 1998;115:58–66.
Akopyants NS, Fradkov A, Diatchenko L et al. PCR-based subtractive hybridization and differences in gene content among strains of Helicobacter pylori. Proc Natl Acad Sci USA. 1998;95:13108–13113.
Achtman M, Azuma T, Berg DE et al. Recombination and clonal groupings within Helicobacter pylori from different geographical regions. Mol Microbiol. 1999;32:459–470.
Suerbaum S, Smith JM, Bapumia K et al. Free recombination within Helicobacter pylori. Proc Natl Acad Sci USA. 1998;95:12619–12624.
Kersulyte D, Chalkauskas H, Berg DE. Emergence of recombinant strains of Helicobacter pylori during human infection. Mol Microbiol. 1999;31:31–43.
Spohn G, Beier D, Rappuoli R, Scarlato V. Transcriptional analysis of the divergent cagAB genes encoded by the pathogenicity island of Helicobacter pylori. Mol Microbiol. 1997;26:361–372.
Wang G, Rasko DA, Sherburne R, Taylor DE. Molecular genetic basis for the variable expression of Lewis Y antigen in Helicobacter pylori: analysis of the alpha (1,2) fucosyltrans-ferase gene. Mol Microbiol. 1999;31:1265–1274.
McGowan CC, Necheva A, Thompson SA, Cover TL, Blaser MJ. Acid-induced expression of an LPS-associated gene in Helicobacter pylori. Mol Microbiol. 1998;30:19–31.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2000 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Michetti, P. (2000). The inflamatory activity in Helicobacter pylori infection is predominantly organism related. In: Hunt, R.H., Tytgat, G.N.J. (eds) Helicobacter pylori. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3927-4_21
Download citation
DOI: https://doi.org/10.1007/978-94-011-3927-4_21
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5753-0
Online ISBN: 978-94-011-3927-4
eBook Packages: Springer Book Archive