Immunological features and the ability of inhibitory effects on enzymatic activity of an epitope vaccine composed of cholera toxin B subunit and B cell epitope from Helicobacter pylori urease A subunit

Guo, Le; Li, Xiaokang; Tang, Feng; He, Yongli; Xing, Yingying; Deng, Xuepeng; Xi, Tao

doi:10.1007/s00253-011-3726-0

Cited by 29 publications

(31 citation statements)

References 31 publications

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“…The detection of antigen-specific antibodies was performed using ELISA, as previously described (Guo et al 2012a). The serum was isolated after the last immunization.…”

Section: Measurement Of Antibody Response Using Elisamentioning

confidence: 99%

A novel chimeric flagellum fused with the multi-epitope vaccine CTB-UE prevents Helicobacter pylori-induced gastric cancer in a BALB/c mouse model

Song

Yang

et al. 2015

Appl Microbiol Biotechnol

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Helicobacter pylori (H. pylori) infection causes peptic ulcers, gastric adenocarcinoma, and mucosa-associated lymphoid tissue (MALT) lymphoma. The eradication of H. pylori might be an effective means of preventing gastric cancer. A dual-antigen epitope and dual-adjuvant vaccine called CTB-UE-CF (CCF) was constructed by combining a multi-epitope vaccine CTB-UE with a novel chimeric flagellum (CF) to simultaneously activate Toll-like receptor (TLR) 5-agonist activity and preserve the immunogenicity of H. pylori flagellum FlaA. The evaluation of efficacy to reduce H. pylori colonization was performed using BALB/c mice by oral immunization with a triple dose of this vaccine strain. Two weeks after the last immunization, mice were sacrificed to determine specific antibody levels and proinflammatory cytokine production. To determine the presence of H. pylori, we detected the number of H. pylori by real-time quantitative PCR (qPCR) and measured the urease activity in the gastric tissue. The results showed that the immunogenicity and mucosal immune responses of CCF performed significantly better than those of CTB-UE. This dual-antigen epitope and dual-adjuvant system might greatly contribute to the development of a safe and efficient therapeutic vaccine for humans against H. pylori infection.

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“…The detection of antigen-specific antibodies was performed using ELISA, as previously described (Guo et al 2012a). The serum was isolated after the last immunization.…”

Section: Measurement Of Antibody Response Using Elisamentioning

confidence: 99%

A novel chimeric flagellum fused with the multi-epitope vaccine CTB-UE prevents Helicobacter pylori-induced gastric cancer in a BALB/c mouse model

Song

Yang

et al. 2015

Appl Microbiol Biotechnol

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“…Both peptides were bound with the linker (DPRVPSS) to avoid the formation of new epitopes. The CTB-UreA epitope vaccine had good immunogenicity and immunoreactivity and induced specific neutralizing antibodies which showed an effectively inhibitory effect on H. pylori urease enzymatic activity [143]. …”

Section: Organic Chemistry Tools In Immune Response Investigationsmentioning

confidence: 99%

Bacterial Urease and its Role in Long-Lasting Human Diseases

Konieczna

Żarnowiec²,

Kwinkowski³

et al. 2012

CPPS

224

155

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Urease is a virulence factor found in various pathogenic bacteria. It is essential in colonization of a host organism and in maintenance of bacterial cells in tissues. Due to its enzymatic activity, urease has a toxic effect on human cells. The presence of ureolytic activity is an important marker of a number of bacterial infections. Urease is also an immunogenic protein and is recognized by antibodies present in human sera. The presence of such antibodies is connected with progress of several long-lasting diseases, like rheumatoid arthritis, atherosclerosis or urinary tract infections. In bacterial ureases, motives with a sequence and/or structure similar to human proteins may occur. This phenomenon, known as molecular mimicry, leads to the appearance of autoantibodies, which take part in host molecules destruction. Detection of antibodies-binding motives (epitopes) in bacterial proteins is a complex process. However, organic chemistry tools, such as synthetic peptide libraries, are helpful in both, epitope mapping as well as in serologic investigations. In this review, we present a synthetic report on a molecular organization of bacterial ureases - genetic as well as structural. We characterize methods used in detecting urease and ureolytic activity, including techniques applied in disease diagnostic processes and in chemical synthesis of urease epitopes. The review also provides a summary of knowledge about a toxic effect of bacterial ureases on human body and about occurrence of anti-urease antibodies in long-lasting diseases.

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“…In this work we continue the use of subunit A of the urease (UreA) of Helicobacter acinonychis [10], which has been used extensively as an antigen able to induce, an immune response [20-24]. In this study we were looking for improvements in spore surface display, and decided to use CotZ as the anchor protein, based on its localisation in the external layer of the outer coat of B. subtilis spores [16].…”

Section: Discussionmentioning

confidence: 99%

New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis

2013

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BackgroundIn last decade spores have been successfully used as a surface display platform. Various peptides or proteins were displayed this way as functional enzymes or antigens. Nearly all attempts involved use of three coat proteins: CotB, CotC or CotG. Increasing knowledge of the structure of the spore coat allowed us to propose the use of other proteins whose localization in the spore envelope has been determined. We also propose the application of a new linker suitable for building fusion proteins.ResultsWe show that a member of the outer coat, CotZ, is a good candidate as a new anchor protein useful in spore surface display. This protein allows use of relatively large passenger proteins and their efficient display on the spore surface. Analysis by Western- and dot-blotting, combined with immunofluorescence microscopy, allowed us to estimate the number of displayed fusion proteins molecules as 1.4 × 102 per spore. In addition, we present data indicating that the use of a peptide linker, which forms a stable α-helix, may greatly improve the display of anchored proteins on the spore surface.ConclusionCotZ can be used as an efficient anchor protein in the outer spore coat. Its localisation in the coat crust layer should guarantee surface display of passenger proteins. Moreover, a CotZ based fusion can tolerate relatively large passenger proteins for efficient spore surface display. In addition, to the properties of both the anchor and passenger proteins, an important issue is the nature of the linker. Here we present evidence that the linker, which forms a stable α-helix, may be crucial for successful display.

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Immunological features and the ability of inhibitory effects on enzymatic activity of an epitope vaccine composed of cholera toxin B subunit and B cell epitope from Helicobacter pylori urease A subunit

Cited by 29 publications

References 31 publications

A novel chimeric flagellum fused with the multi-epitope vaccine CTB-UE prevents Helicobacter pylori-induced gastric cancer in a BALB/c mouse model

A novel chimeric flagellum fused with the multi-epitope vaccine CTB-UE prevents Helicobacter pylori-induced gastric cancer in a BALB/c mouse model

Bacterial Urease and its Role in Long-Lasting Human Diseases

New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis

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