Immunity and Vaccine Development Against Helicobacter pylori

2019 ◽  
pp. 257-275 ◽  
Author(s):  
Anna K. Walduck ◽  
Sukanya Raghavan
Keyword(s):  
Helicobacter Pylori ◽  
Vaccine Development

A multi-method and structure-based in silico vaccine designing against Helicobacter pylori employing immuno-informatics approach

2020 ◽  
Vol 17 ◽  
Author(s):  
Anam Naz ◽  
Tahreem Zaheer ◽  
Hamza Arshad Dar ◽  
Faryal Mehwish Awan ◽  
Ayesha Obaid ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Vaccine Development ◽  
Amino Acid Sequences ◽  
The Body ◽  
New Drugs ◽  
Toll Like Receptor ◽  
Peptide Vaccines ◽  
Hla Alleles ◽  
Vaccine Candidates ◽  
H Pylori

Background: Helicobacter pylori infection and its treatment still remains a challenge to human health worldwide. A variety of antibiotics and combination therapies are currently used to treat H. pylori induced ulcers and carcinoma; however, no effective treatment is available to eliminate the pathogen from the body. Additionally, antibiotic resistance is also one of the main reasons for prolonged and persistent infection. Aim of the study: Until new drugs are available for this infection, vaccinology seems the only alternative opportunity to exploit against H. pylori induced diseases. Methods: Multiple epitopes prioritized in our previous study have been tested for their possible antigenic combinations, and results in 169-mer and 183-mer peptide vaccines containing the amino acid sequences of 3 and 4 epitopes respectively, along with adjuvant (Cholera Toxin Subunit B adjuvant at 5’ end) and linkers (GPGPG and EAAAK). Results: Poly-epitope proteins proposed as potential vaccine candidates against H. pylori include SabAHP0289-Omp16-VacA (SHOV), VacA-Omp16-HP0289-FecA (VOHF), VacA-Omp16-HP0289-SabA (VOHS), VacA-Omp16-HP0289-BabA (VOHB), VacA-Omp16-HP0289-SabA-FecA (VOHSF), VacAOmp16-HP0289-SabA-BabA (VOHSB) and VacA-Omp16-HP0289-BabA-SabA (VOHBS). Structures of these poly-epitope peptide vaccines have been modelled and checked for their affinity with HLA alleles and receptors. These proposed poly-epitope vaccine candidates bind efficiently with A2, A3, B7 and DR1 superfamilies of HLA alleles. They can also form stable and significant interactions with Toll-like receptor 2 and Toll-like receptor 4. Conclusion: Results suggest that these multi-epitopic vaccines can elicit a significant immune response against H. pylori and can be tested further for efficient vaccine development.

scholarly journals Multiparameter Selection of Helicobacter pylori Antigens Identifies Two Novel Antigens with High Protective Efficacy

2002 ◽  
Vol 70 (11) ◽  
pp. 6499-6503 ◽  
Author(s):  
N. Sabarth ◽  
R. Hurwitz ◽  
T. F. Meyer ◽  
D. Bumann
Keyword(s):  
Helicobacter Pylori ◽  
Protective Immunity ◽  
Vaccine Development ◽  
Protective Efficacy ◽  
Infection Model ◽  
Protective Antigens ◽  
High Yields ◽  
Selection Of

ABSTRACT A multiparameter selection of Helicobacter pylori antigens for vaccine development identified 15 candidates, 6 of which are known protective antigens. Two novel antigens with low homology to other organisms (HP0231 and HP0410) were overexpressed and purified with high yields. Both confer protective immunity in the mouse Helicobacter infection model.

Peroral immunization with Helicobacter pylori adhesin protein genetically linked to cholera toxin A2B subunits

2001 ◽  
Vol 100 (3) ◽  
pp. 291-298 ◽  
Author(s):  
Byung Oh KIM ◽  
Sung Seup SHIN ◽  
Young Hyo YOO ◽  
Suhkneung PYO
Keyword(s):  
Helicobacter Pylori ◽  
Cholera Toxin ◽  
Vaccine Development ◽  
Protective Antigen ◽  
Oral Immunization ◽  
Size Exclusion ◽  
Vaccine Antigen ◽  
Igg Antibodies ◽  
Serum Igg ◽  
H Pylori

Helicobacter pylori is a major cause of gastric-associated diseases. To evaluate the efficacy of a possible vaccine antigen against H. pylori infection, the chimaeric construct adhesin–CTXA2B, derived from H. pylori adhesin genetically coupled to cholera toxin (CTX) subunits A2 and B (CTXA2B), was expressed in Escherichia coli as an insoluble recombinant chimaeric protein. The protein was then purified by denaturation, renaturation and size-exclusion chromatography. The composition of purified adhesin–CTXA2B was verified by SDS/PAGE and Western blotting with antibodies to antigenic components of adhesin and CTXB, and confirmed as a chimaeric protein with GM1-ganglioside binding activity and adhesin epitopes by a GM1-ELISA developed using antibodies to adhesin. Oral immunization of mice with adhesin–CTXA2B induced higher levels of mucosal IgA and serum IgG antibodies to H. pylori adhesin and to CTXB than in mice immunized with adhesin or CTXA2B alone. Adhesin–CTXA2B was also demonstrated to be a potential protective antigen in a mouse model of H. pylori infection. The immunization of mice with adhesin–CTXA2B protected 62.5% of mice infected with H. pylori SS1 strain, whereas adhesin immunization was not able to confer protection to mice. This protection may be correlated with high levels of mucosal IgA and serum IgG antibodies against H. pylori adhesin. Taken together, the results indicate that the genetically linked CTXA2B acts as a useful mucosal adjuvant, and that the adhesin–CTXA2B chimaeric protein could be a potential component in future H. pylori vaccine development.

scholarly journals Generation and Characterization of Human Monoclonal scFv Antibodies against Helicobacter pylori Antigens

2002 ◽  
Vol 70 (8) ◽  
pp. 4158-4164 ◽  
Author(s):  
Nicole Reiche ◽  
Andreas Jung ◽  
Thomas Brabletz ◽  
Tanja Vater ◽  
Thomas Kirchner ◽  
...  
Keyword(s):  
Immune Response ◽  
Helicobacter Pylori ◽  
Phage Display ◽  
Humoral Immune Response ◽  
Vaccine Development ◽  
Enzyme Linked Immunosorbent Assay ◽  
Single Chain ◽  
Humoral Immune ◽  
Single Chain Fv ◽  
H Pylori

ABSTRACT Infection with Helicobacter pylori is chronic despite a vigorous cellular and humoral immune response and causes severe pathology in some patients. In this study, phage display was used as a new approach in order to investigate the role of the host's humoral immune response in the pathogenesis of H. pylori gastritis. Human monoclonal single-chain Fv (scFv) antibody fragments against H. pylori cell lysate and the H. pylori urease were isolated from an immune phage display library, constructed from peripheral blood lymphocytes of an H. pylori-infected patient. After affinity selection, 23% of the clones tested showed binding activity against a lysate of the H. pylori Sydney strain in enzyme-linked immunosorbent assay (ELISA) and 9% bound the H. pylori urease. Further characterization by PCR-fingerprint analysis and sequencing revealed that two closely related H. pylori binders and one antiurease scFv could be isolated. The selected scFvs were highly specific as analyzed by ELISA and immunoblots using various bacterial lysates and recombinant proteins. Analysis of the humoral immune response following H. pylori infection using human monoclonal antibodies might contribute to a better understanding of the pathogenesis of the disease. Moreover, using immune phage display libraries, it might be possible for relevant epitopes of H. pylori antigens to be determined, which might be of use for vaccine development.

scholarly journals Relevance of Helicobacter pylori virulence factors for vaccine development

2009 ◽  
Vol 51 ◽  
pp. s447-s454 ◽  
Author(s):  
Luz del Carmen Hernández-Hernández ◽  
Eduardo César Lazcano-Ponce ◽  
Yolanda López-Vidal ◽  
Germán Rubén Aguilar-Gutiérrez
Keyword(s):  
Helicobacter Pylori ◽  
Virulence Factors ◽  
Vaccine Development

scholarly journals B-Cell and T-Cell Immune Responses to Experimental Helicobacter pylori Infection in Humans

2005 ◽  
Vol 73 (5) ◽  
pp. 2999-3006 ◽  
Author(s):  
Zhannat Z. Nurgalieva ◽  
Margaret E. Conner ◽  
Antone R. Opekun ◽  
Carl Q. Zheng ◽  
Susan N. Elliott ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
T Cell ◽  
Vaccine Development ◽  
Immunoglobulin M ◽  
T Cell Subsets ◽  
Cell Immune Response ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Igm Antibody ◽  
H Pylori

ABSTRACT The acute antibody and T-cell immune response to Helicobacter pylori infection in humans has not been studied systematically. Serum from H. pylori-naive volunteers challenged with H. pylori and cured after 4 or 12 weeks was tested by enzyme-linked immunosorbent assays for anti-H. pylori-specific immunoglobulin M (IgM) and IgA established using bacterial lysates from homologous (the infecting strain) and heterologous H. pylori. Proteins recognized by IgM antibody were identified by mass spectrometry of immunoreactive bands separated by two-dimensional gel electrophoresis. Mucosal T-cell subsets (CD4, CD8, CD3, and CD30 cells) were assessed by immunohistochemistry. All 18 infected volunteers developed H. pylori-specific IgM responses to both homologous or heterologous H. pylori antigens. H. pylori antigens reacted with IgM antibody at 4 weeks postinfection. IgM Western blotting showed immunoreactivity of postinfection serum samples to multiple H. pylori proteins with molecular weights ranging between 9,000 (9K) to 150K with homologous strains but only a 70K band using heterologous antigens. Two-dimensional electrophoresis demonstrated that production of H. pylori-specific IgM antibodies was elicited by H. pylori flagellins A and B, urease B, ABC transporter binding protein, heat shock protein 70 (DnaK), and alkyl hydroperoxide reductase. Mucosal CD3, CD4, and CD8 T-cell numbers increased following infection. IgM antibody responses were detected to a range of homologous H. pylori antigens 2 to 4 weeks postchallenge. The majority of H. pylori proteins were those involved in motility and colonization and may represent targets for vaccine development.

Sign in / Sign up

Export Citation Format

Share Document