Characterization of murine T-cell epitopes on mycobacterial DNA-binding protein 1 (MDP1) using DNA vaccination

Suzuki, Daisuke; Nagata, Toshi; Eweda, Ghada; Matsumoto, Sohkichi; Matsumoto, Makoto; Tsujimura, Kunio; Koide, Yukio

doi:10.1016/j.vaccine.2009.10.062

Cited by 7 publications

(3 citation statements)

References 32 publications

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“…Several CD4+ and one CD8+ T-cell epitopes were identified on the DNA-binding protein 1 (MDP1) antigen (95), while spleen CD4 T cells from HLA-DRB1*0401 transgenic mice recognized only the p191–210 epitope on the MPT51 antigen (96). A fusion DNA vaccine incorporating the HSP70 C-terminal domain (as adjuvant) and MPT51 (as target antigen) stimulated CD4, but not the CD8 T-cell response (97).…”

Section: Peptide Epitope-based Vaccination Against Tbmentioning

confidence: 99%

Function and Potentials of M. tuberculosis Epitopes

Iványi

2014

Front. Immunol.

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Study of the function of epitopes of Mycobacterium tuberculosis antigens contributed significantly toward better understanding of the immunopathogenesis and to efforts for improving infection and disease control. Characterization of genetically permissively presented immunodominant epitopes has implications for the evolution of the host–parasite relationship, development of immunodiagnostic tests, and subunit prophylactic vaccines. Knowledge of the determinants of cross-sensitization, relevant to other pathogenic or environmental mycobacteria and to host constituents has advanced. Epitope-defined IFNγ assay kits became established for the specific detection of infection with tubercle bacilli both in humans and cattle. The CD4 T-cell epitope repertoire was found to be more narrow in patients with active disease than in latently infected subjects. However, differential diagnosis of active TB could not be made reliably merely on the basis of epitope recognition. The mechanisms by which HLA polymorphism can influence the development of multibacillary tuberculosis (TB) need further analysis of epitopes, recognized by Th2 helper cells for B-cell responses. Future vaccine development would benefit from better definition of protective epitopes and from improved construction and formulation of subunits with enhanced immunogenicity. Epitope-defined serology, due to its operational advantages is suitable for active case finding in selected high disease incidence populations, aiming for an early detection of infectious cases and hence for reducing the transmission of infection. The existing knowledge of HLA class I binding epitopes could be the basis for the construction of T-cell receptor-like ligands for immunotherapeutic application. Continued analysis of the functions of mycobacterial epitopes, recognized by T cells and antibodies, remains a fertile avenue in TB research.

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Section: Peptide Epitope-based Vaccination Against Tbmentioning

confidence: 99%

Function and Potentials of M. tuberculosis Epitopes

Iványi

2014

Front. Immunol.

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“…T-cell responses specific for HspX were found in latent Mtb infection (Demissie et al, 2006). In addition, mycobacterial DNA-binding protein-1 (MDP1) has been shown to be expressed in the late phase of TB and induce humoral and cellular immune responses (Matsumoto et al, 2005;Suzuki et al, 2010). Analysis of dormant phase proteins is critical for development of therapeutic TB vaccines against persistent Mtb infection.…”

Section: Dormant Phase Proteinsmentioning

confidence: 99%

Immune Responses Against Mycobacterium

Nagata¹,

Koide²

2012

Understanding Tuberculosis - Analyzing the Origin of Mycobacterium Tuberculosis Pathogenicity

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“…This would provide clues and help for future studies. We combined bioinformatic predictions and experimental validation, a method which is widely used and has successfully identified many antigen epitopes, for the screening and identification of H-2 restricted T cell epitopes on the FMDV structural protein VP1 [25-29]. Additionally, it was used to successfully identify possible CTL T cell epitopes on two FMDV structural proteins VP1.…”

Section: Introductionmentioning

confidence: 99%

Identification of H-2d Restricted T Cell Epitope of Foot-and-mouth Disease Virus Structural Protein VP1

Liu

Wang

Zhang

et al. 2011

Virol J

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BackgroundFoot-and-mouth disease (FMD) is a highly contagious and devastating disease affecting livestock that causes significant financial losses. Therefore, safer and more effective vaccines are required against Foot-and-mouth disease virus(FMDV). The purpose of this study is to screen and identify an H-2d restricted T cell epitope from the virus structural protein VP1, which is present with FMD. We therefore provide a method and basis for studying a specific FMDV T cell epitope.ResultsA codon-optimized expression method was adopted for effective expression of VP1 protein in colon bacillus. We used foot-and-mouth disease standard positive serum was used for Western blot detection of its immunogenicity. The VP1 protein was used for immunizing BALB/c mice, and spleen lymphocytes were isolated. Then, a common in vitro training stimulus was conducted for potential H-2Dd, H-2Kd and H-2Ld restricted T cell epitope on VP1 proteins that were predicted and synthesized by using a bioinformatics method. The H-2Kd restricted T cell epitope pK1 (AYHKGPFTRL) and the H-2Dd restricted T cell epitope pD7 (GFIMDRFVKI) were identified using lymphocyte proliferation assays and IFN-γ ELISPOT experiments.ConclusionsThe results of this study lay foundation for studying the FMDV immune process, vaccine development, among other things. These results also showed that, to identify viral T cell epitopes, the combined application of bioinformatics and molecular biology methods is effective.

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Characterization of murine T-cell epitopes on mycobacterial DNA-binding protein 1 (MDP1) using DNA vaccination

Cited by 7 publications

References 32 publications

Function and Potentials of M. tuberculosis Epitopes

Function and Potentials of M. tuberculosis Epitopes

Immune Responses Against Mycobacterium

Identification of H-2d Restricted T Cell Epitope of Foot-and-mouth Disease Virus Structural Protein VP1

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