Comparative proteomics and immunoproteomics of Helicobacter pylori related to different gastric pathologies☆

Mini, Roberta; Bernardini, Giulia; Salzano, Anna Maria; Renzone, Giovanni; Scaloni, Andrea; Figura, Natale; Santucci, Annalisa

doi:10.1016/j.jchromb.2005.12.052

Cited by 34 publications

(50 citation statements)

References 59 publications

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“…Interestingly, some of the proteins identified as antigens in this study have been previously identified as antigenic in other settings, and, in each case, their antigenic domains have been mapped to protein sites [47,[51][52][53]. Furthermore, 15 of the putative antigens were identified from multiple closely associated spots, suggesting that varying degrees of PTM were present, but that antigenicity was not dependent on PTM [44,45,47,49]. Additional studies will be necessary to both confirm xenogeneic antigenicity and identify the specific antigenic domain of each identified putative xenoantigen.…”

Section: Discussionmentioning

confidence: 75%

“…This approach led to the identification of 31 putative antigenic proteins capable of eliciting a T cell-dependent antibody response, as revealed by IgG production [42,43]. Similar approaches have been used recently to identify relevant antigenic proteins in oncologic, autoimmune, and infectious diseases [44][45][46][47][48][49][50]. To our knowledge, this study is the first to apply an immunoproteomic approach to identify potential antigens in xenotransplanted tissues.…”

Section: Discussionmentioning

confidence: 86%

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Immunoproteomic identification of bovine pericardium xenoantigens

et al. 2008

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Bovine pericardium is an important biomaterial with current application in glutaraldehyde-fixed bioprosthetic heart valves and possible future application as an unfixed biological scaffold for tissue engineering. The importance of both humoral and cell-mediated rejection responses toward fixed and unfixed xenogeneic tissues has become increasingly apparent. However, the full scope and specific identities of bovine pericardium proteins that can elicit an immune response remain largely unknown. In this study, an immunoproteomic approach was used to survey bovine pericardium proteins for their ability to elicit a humoral immune response in rabbits. A two-stage protein extraction protocol was used to separate bovine pericardium proteins into water-and lipid-soluble fractions. Two-dimensional gel electrophoresis was performed to separate the proteins from each fraction. Western blots were generated from two-dimensional gels of both bovine pericardium protein fractions. These blots were probed with serum from rabbits immunized with bovine pericardium and a secondary antibody was used to assess for IgG positivity. Western blots were compared to duplicate two-dimensional gels and proteins in matched spots were identified by tandem mass spectrometry. Thirty-one putative protein antigens were identified, eight of which are known to be antigenic from previous studies. All of the putative antigens demonstrated progressive staining intensity with increasing days of post-exposure serum. Identified antigenic proteins represented a variety of functional and structural protein types, and included both cellular and matrix proteins. The results of this study have implications for the use of bovine pericardium as a biomaterial in bioprostheses and tissue engineering applications, as well as xenotransplantation in general.

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Section: Discussionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 86%

Immunoproteomic identification of bovine pericardium xenoantigens

et al. 2008

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“…Proteomics approaches have been used to map protein patterns of multiple H. pylori strains, and a number of studies have reported immunoproteomic approaches to identify antigenic proteins (Mini et al, 2006;. Proteome technology using 2-DE gel by ESI-MS-MS has been used to identify four H. pylori immunogenic low-molecular-weight (25-30 KDa) proteins: UreA, cell binding factor 2, hypothetical protein and outer membrane protein.…”

Section: Discussionmentioning

confidence: 99%

Antigenic Proteins of Helicobacter pylori of Potential Diagnostic Value

Khalilpour

Agilan²,

Lee³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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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 (≥ 70%) sensitivity and high specificity (98-100%) towards anti-Helicobacter IgG antibody in culturepositive 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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“…Jungblut et al and Haas et al screened the proteome of H. pylori 26695 using single sera and determined differences in the immune response of patients with various clinical manifestations [16,19,23,34]. Furthermore, comparative analysis conducted by Mini et al revealed a significant heterogeneity between selected antigens that is dependent on both the bacterial strain and the sera used for analysis [38]. Comparison of the provided data presents difficulties, due mainly to the genetic diversity of H. pylori as well as to methodological differences.…”

Section: Introductionmentioning

confidence: 99%

Tip-α (hp0596 Gene Product) Is a Highly Immunogenic Helicobacter pylori Protein Involved in Colonization of Mouse Gastric Mucosa

et al. 2008

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A product of the Helicobacter pylori hp0596 gene (Tip-a) is a highly immunogenic homodimeric protein, unique for this bacterium. Cell fractionation experiments indicate that Tip-a is anchored to the inner membrane. In contrast, the three-dimensional model of the protein suggests that Tip-a is soluble or, at least, largely exposed to the solvent. hp0596 gene knockout resulted in a significant decrease in the level of H. pylori colonization as measured by real-time PCR assay. In addition, the Tip-a recombinant protein was determined to stimulate macrophage to produce IL-1a and TNF-a. Both results imply that Tip-a is rather loosely connected to the inner membrane and potentially released during infection.

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Comparative proteomics and immunoproteomics of Helicobacter pylori related to different gastric pathologies☆

Cited by 34 publications

References 59 publications

Immunoproteomic identification of bovine pericardium xenoantigens

Immunoproteomic identification of bovine pericardium xenoantigens

Antigenic Proteins of Helicobacter pylori of Potential Diagnostic Value

Tip-α (hp0596 Gene Product) Is a Highly Immunogenic Helicobacter pylori Protein Involved in Colonization of Mouse Gastric Mucosa

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