InSilico Identification and Conservation Analysis of B-cell and T-Cell Epitopes of Hepatitis C Virus 3a Genotype Enveloped Glycoprotein 2From Pakistan: A Step Towards Heterologous Vaccine Design

Ikram, Aqsa; Anjum, Sadia; Tahir, Muhammad

doi:10.5812/hepatmon.9832

Cited by 13 publications

(10 citation statements)

References 31 publications

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“…But this peptide had no high antigenicity score in the present study (29). In a similar study, Ikram et al confirmed that many epitopes from E2 protein are conserved in HCV 3a genotypes and HCV gpE2 is an ideal target for HCV vaccine design (30). In another study more probable and conserved T-and B-cell epitopes of E1 protein from HCV isolated in Pakistan were introduced as potential B-and T-cell epitopes that can raise the desired immune response against HCV (31).…”

Section: Discussionmentioning

confidence: 43%

A Novel Multi-Epitope Vaccine For Cross Protection Against Hepatitis C Virus (HCV): An Immunoinformatics Approach

2017

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Background: Hepatitis C virus (HCV) causes acute and chronic human hepatitis infections. Due to the high genetic diversity and high rates of mutations in the genetic material, so far there has been no approved vaccine against HCV. Materials and Methods: The aim of this study was to determine conserved Band T-cell epitopes of E1 and E2 proteins from HCV and to construction a chimeric peptide as a novel epitope-based vaccine for cross-protection against the virus. To this end, one B-and one T-cell epitope from both E1 and E2 which were predicted by EPMLR and Propred-1 server and had the highest score and antigenicity in VaxiJen 2.0 and PAP servers were selected for the construction of chimeric protein as a multi-epitope vaccine. Results:The results of this study showed that the chimeric peptide had a high antigenicity score and stability. Results also showed that most epitopes of E1 were located in two spectra consist of 45-65, 88-107 and 148-182 while the results of Bcell epitopes of E2 showed that this protein had fewer epitopes than E1. The epitopes predicted for E2 were located in (12-24 and 35-54) spectra. Conclusion:In conclusion, epitope-based vaccine which was designed by immunoinformatics methods could be considered as a novel and effective vaccine for cross-protection against HCV infection.

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Section: Discussionmentioning

confidence: 43%

A Novel Multi-Epitope Vaccine For Cross Protection Against Hepatitis C Virus (HCV): An Immunoinformatics Approach

2017

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“…Most of the prediction of epitopes are based on E2 sequence (Ikram, Anjum, & Tahir, 2014) not for the HCV [E1.E2] complex. Our result shows 18 sequential epitopes present in the sequence of [E1.E2] that is part of our model (Table 3).…”

Section: Resultsmentioning

confidence: 99%

Structure–function analysis of hepatitis C virus envelope glycoproteins E1 and E2

Nayak¹,

Pattabiraman²,

Fadra³

et al. 2014

Journal of Biomolecular Structure and Dynamics

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Hepatitis C virus (HCV) is the leading cause of chronic liver disease in humans. The envelope proteins of HCV are potential candidates for vaccine development. The absence of three-dimensional (3D) structures for the functional domain of HCV envelope proteins [E1.E2] monomer complex has hindered overall understanding of the virus infection, and also structure-based drug design initiatives. In this study, we report a 3D model containing both E1 and E2 proteins of HCV using the recently published structure of the core domain of HCV E2 and the functional part of E1, and investigate immunogenic implications of the model. HCV [E1.E2] molecule is modeled by using aa205–319 of E1 to aa421–716 of E2. Published experimental data were used to further refine the [E1.E2] model. Based on the model, we predict 77 exposed residues and several antigenic sites within the [E1.E2] that could serve as vaccine epitopes. This study identifies eight peptides which have antigenic propensity and have two or more sequentially exposed amino acids and 12 singular sites are under negative selection pressure that can serve as vaccine or therapeutic targets. Our special interest is 285FLVGQLFTFSPRRHW299 which has five negatively selected sites (L286, V287, G288, T292, and G303) with three of them sequential and four amino acids exposed (F285, L286, T292, and R296). This peptide in the E1 protein maps to dengue envelope vaccine target identified previously by our group. Our model provides for the first time an overall view of both the HCV envelope proteins thereby allowing researchers explore structure-based drug design approaches.

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“…To enhance the immunogenicity of CD8+ T-cell responses, a Th CD4+ epitope (HLA-DR) from NS3 (NS31248-1262) was also chosen. Since clearance of HCV infection is associated with early appearance of broad neutralizing antibody responses, a neutralizing B-cell epitope from E2 (E2412-426) conserved between genotypes of HCV was considered for incorporation into the set of epitopes ( 25 , 26 , 32 ).…”

Section: Methodsmentioning

confidence: 99%

Immunogenicity of Multi-Epitope DNA and Peptide Vaccine Candidates Based on Core, E2, NS3 and NS5B HCV Epitopes in BALB/c Mice

et al. 2014

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Background:Hypervariability of HCV proteins is an important obstacle to design an efficient vaccine for HCV infection. Multi-epitope vaccines containing conserved epitopes of the virus could be a promising approach for protection against HCV.Objectives:Cellular and humoral immune responses against multi-epitope DNA and peptide vaccines were evaluated in BALB/c mice.Materials and Methods:In this experimental study, multi-epitope DNA- and peptide-based vaccines for HCV infection harboring immunodominant CD8+ T cell epitopes (HLA-A2 and H2-Dd) from Core (132-142), NS3 (1073-1081) and NS5B (2727-2735), a Th CD4+ epitope from NS3 (1248-1262) and a B-cell epitope from E2 (412-426) were designed. Multi-epitope DNA and peptide vaccines were tested in two regimens as heterologous DNA/peptide (group 1) and homologous peptide/peptide (group 2) prime/boost vaccine in BALB/c mice model. Electroporation was used for delivery of the DNA vaccine. Peptide vaccine was formulated with Montanide ISA 720 (M720) as adjuvant. Cytokine assay and antibody detection were performed to analyze the immune responses.Results:Mice immunized with multi-epitope peptide formulated with M720 developed higher HCV-specific levels of total IgG, IgG1 and IgG2a than those immunized with multi-epitope DNA vaccine. IFN-γ levels in group 2 were significantly higher than group 1 (i.e. 3 weeks after the last immunization; 37.61 ± 2.39 vs. 14.43 ± 0.43, P < 0.05). Moreover, group 2 had a higher IFN-γ/IL-4 ratio compared to group 1, suggesting a shift toward Th1 response. In addition, in the present study, induced immune responses were long lasting and stable after 9 weeks of the last immunization.Conclusions:Evaluation of multi-epitope DNA and peptide-vaccines confirmed their specific immunogenicity in BALB/c mice. However, lower Th1 immune responses in mice immunized with DNA vaccine suggests further investigations to improve the immunogenicity of the multi-epitope DNA vaccine through immune enhancers.

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InSilico Identification and Conservation Analysis of B-cell and T-Cell Epitopes of Hepatitis C Virus 3a Genotype Enveloped Glycoprotein 2From Pakistan: A Step Towards Heterologous Vaccine Design

Cited by 13 publications

References 31 publications

A Novel Multi-Epitope Vaccine For Cross Protection Against Hepatitis C Virus (HCV): An Immunoinformatics Approach

A Novel Multi-Epitope Vaccine For Cross Protection Against Hepatitis C Virus (HCV): An Immunoinformatics Approach

Structure–function analysis of hepatitis C virus envelope glycoproteins E1 and E2

Immunogenicity of Multi-Epitope DNA and Peptide Vaccine Candidates Based on Core, E2, NS3 and NS5B HCV Epitopes in BALB/c Mice

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