Expression and immunogenic analysis of recombinant polypeptides derived from capsid protein VP1 for developing subunit vaccine material against hepatitis A virus

Jang, Kyoung Ok; Park, Jong-Hwa; Lee, Hyun Ho; Chung, Dae Kyun; Kim, Wonyong; Chung, In Sik

doi:10.1016/j.pep.2014.04.011

Cited by 6 publications

(3 citation statements)

References 18 publications

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“…In general, linker sequences were inserted between different epitopes to make each epitope possible to induce immune response (Tian et al, 2014). For example, based on this principle, recombinant linear neutralizing epitope tandem of human enterovirus 71 and polypeptides derived from capsid protein VP1 were expressed in Escherichia coli, followed by producing specific mouse neutralization antibodies (IgG) against the recombinant protein (Jang et al, 2014;Li et al, 2014). Moreover, specific antibodies were produced against all the epitopes of a recombinant epitope tandem protein derived from Helicobacter pylori urease (Guo et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovineβ-lactoglobulin

He¹,

Gao

et al. 2016

Food and Agricultural Immunology

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Bovine β-lactoglobulin (BLG) is one of the major allergens in cow's milk. Epitopes play a key role in food allergy, while most of the antibodies developed do not specifically recognize the IgEbinding epitopes. Here, a tandem derived from human IgE linear epitopes of BLG (tBLG) was designed according to the principles of epitope-based vaccine methodology, expressed in Escherichia coli, and a polyclonal antibody (pAb-tBLG) was developed. The recombinant tBLG protein preserved the antigenicity and potential allergenicity of epitopes. The pAb-tBLG recognized all the IgE epitopes of tBLG, and showed a high specificity, but it had weak cross-reactivity with caseins. We concluded that pAb-tBLG can detect of BLG and may be useful for identifying allergenic residues in dairy products.

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Section: Introductionmentioning

confidence: 99%

Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovineβ-lactoglobulin

He¹,

Gao

et al. 2016

Food and Agricultural Immunology

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“…Subsequently, intraperitoneal immunization successfully induced the production of specific IgG antibodies against the polypeptides, while also inducing the secretion of IFN-γ and IL-6 in spleen cells. The sera obtained from mice immunized with the recombinant protein showed neutralization activity against HAV [39].…”

Section: Discussionmentioning

confidence: 99%

Expression and Evaluation of a Novel HAV-VP1 and HBS-Ag Fusion Protein for Potential Applications in Immunization and Diagnosis

Hannan,

Jabalameli,

Aghasadeghi

et al. 2023

JoMMID

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Introduction: Hepatitis A virus (HAV) is a causative agent of acute hepatitis in humans, infecting more than one million individuals every year, including both symptomatic and asymptomatic infections. The currently available preventive vaccines for HAV are based on either wild-type or live-attenuated virus strains, which can contribute to the costliness of the vaccination process. Therefore, it may be worthwhile to explore the potential of subunit vaccines that utilize immunogenic viral products. Methods: This study presents the results of a novel recombinant protein production study that employed the native structures of HAV-VP1 and HBs-Ag. The fusion protein underwent comprehensive characterization to evaluate its potential applications in diagnostics and immunization. The truncated recombinant protein, HAV-VP1 (position 99-259 aa) -HBs-Ag, was successfully expressed in the Escherichia coli BL21-DE3 system. Results: The recombinant protein, with a molecular weight of 46 kDa, was evaluated using SDS-PAGE gel electrophoresis and confirmed by western blotting. The fusion protein was successfully detected in serum samples positive for HBV or HAV using anti-HBs and anti-VP1 antibodies. Additionally, it elicited a potent humoral response in BALB/c mice. Conclusion: The novel recombinant protein described in this study has the potential to serve as a bivalent vaccine against HAV and HBV infections. The next step involves evaluating the immunogenicity and safety profile of the protein.

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“…A recombinant subunit vaccine formulated using a fusion protein between Ag85B and ESAT‐6 was shown to be highly protective against Mycobacterium tuberculosis (the causative agent of tuberculosis) in mice [26]. Further examples include development of subunit vaccines to protect against dengue virus,[27] hepatitis A virus,[28] human immunodeficiency virus,[29] human rotavirus,[30] human respiratory syncytial virus,[31] H1N1 influenza virus,[32] Pseudomonas aeruginosa infection[33] and schistosomiasis [34]. All these examples use E. coli as the recombinant host and illustrate the importance of this prokaryotic microbe as a tool in vaccine development.…”

Section: Recombinant Antigen Synthesis Is Possible In a Range Of Hostmentioning

confidence: 99%

Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?

Bill

2014

Journal of Pharmacy and Pharmacology

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Objectives Recombinant protein subunit vaccines are formulated using protein antigens that have been synthesized in heterologous host cells. Several host cells are available for this purpose, ranging from Escherichia coli to mammalian cell lines. This article highlights the benefits of using yeast as the recombinant host. Key findings The yeast species, Saccharomyces cerevisiae and Pichia pastoris, have been used to optimize the functional yields of potential antigens for the development of subunit vaccines against a wide range of diseases caused by bacteria and viruses. Saccharomyces cerevisiae has also been used in the manufacture of 11 approved vaccines against hepatitis B virus and one against human papillomavirus; in both cases, the recombinant protein forms highly immunogenic virus-like particles. Summary Advances in our understanding of how a yeast cell responds to the metabolic load of producing recombinant proteins will allow us to identify host strains that have improved yield properties and enable the synthesis of more challenging antigens that cannot be produced in other systems. Yeasts therefore have the potential to become important host organisms for the production of recombinant antigens that can be used in the manufacture of subunit vaccines or in new vaccine development.

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Expression and immunogenic analysis of recombinant polypeptides derived from capsid protein VP1 for developing subunit vaccine material against hepatitis A virus

Cited by 6 publications

References 18 publications

Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovineβ-lactoglobulin

Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovineβ-lactoglobulin

Expression and Evaluation of a Novel HAV-VP1 and HBS-Ag Fusion Protein for Potential Applications in Immunization and Diagnosis

Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?

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