A novel method for enhancement of peptide vaccination utilizing T-cell epitopes from conventional vaccines

Yano, Akira; Miwa, Yoshikatsu; Kanazawa, Yoshito; Ito, Kaori; Makino, Mitsuhiro; Imai, Shoichi; Hanada, Nobuhiro; Nisizawa, Tosiki

doi:10.1016/j.vaccine.2012.12.083

Cited by 12 publications

(8 citation statements)

References 16 publications

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“…Theoretically, one can consider the analog of the CC36 peptide with the different pI level as a candidate for the development of a vaccine against PrPSc. It was shown that antibodies against the pathological (beta structural) Alzheimer's peptide are effective in slowing down the progression of this disease . So, the antibodies against the pathological (beta structural) form of the prion protein should also prevent the development of the disease.…”

Section: Discussionmentioning

confidence: 99%

“…Another strategy to obtain a stronger immune response to that peptide is to make a synthetic construct composed of the B‐cell epitope of the peptide and T‐cell epitopes of the widespread antigen, such as diphtheria toxin . From this point of view, the CC36 peptide may be considered as a carrier of some B‐cell and T‐cell epitopes of PrPSc but not an infective prion peptide.…”

Section: Discussionmentioning

confidence: 99%

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The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein

et al. 2016

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Mechanisms of beta sheet formation by the human prion protein are not clear yet. In this work, we clarified the role of the region containing C-half of the second helix and N-half of the third helix of that protein in the process of alpha helix to beta sheet transition. Solid phase automatic synthesis of the original peptide (CC36: Cys179-Cys214) failed because of the beta hairpin formation in the region 206-MERVVEQMC-214 with a high beta strand potential. Using Met206Arg and Val210Arg substitutions, we increased the probability of alpha helix formation by that sequence. After that modification, the complete CC36 peptide with disulfide bond has been synthesized. Modified peptide has been studied by circular dichroism (CD) and fluorescence spectrography. According to the CD spectra analysis, the CC36 peptide contains 37% of residues in beta sheet and just 15% in helix. Thermal analysis under the control of CD shows that the secondary structure content of the peptide is stable from 5°C to 80°C. Dissociation of oligomers of the CC36 peptide finishes at 37°C according to the fluorescence analysis. The CC36 peptide is able to bind Mn(2+) cations, which causes small temperature-associated structural shifts at concentrations of 2 - 10·10(-6) M. Predicted beta hairpin of the CC36 peptide (two beta strands are: 184-IKQHTVT-190 and 197-TETDVKM-205) should be the part of a longer beta hairpin from the scrapie form of the prion protein (PrPSc). Analogs of the CC36 peptide may be considered as antigens for the future development of a vaccine against PrPSc. Proteins 2016; 84:1462-1479. © 2016 Wiley Periodicals, Inc.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein

et al. 2016

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“…In the peptide reported in this work, the sequence IAI is between residues 216 and 225 of the subunit 1 of the HA (3LZG). Rothbard and coworkers reported an extensive analysis of the DR1 epitopes, proposing different sequences and combinations of residues that could be recognized . More recently, Yano and coworkers suggested the use of RGD sequence in vaccine design .…”

Section: Discussionmentioning

confidence: 99%

A continuous peptide epitope reacting with pandemic influenza AH1N1 predicted by bioinformatic approaches

et al. 2015

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Computational identification of potential epitopes with an immunogenic capacity challenges immunological research. Several methods show considerable success, and together with experimental studies, the efficiency of the algorithms to identify potential peptides with biological activity has improved. Herein, an epitope was designed by combining bioinformatics, docking, and molecular dynamics simulations. The hemagglutinin protein of the H1N1 influenza pandemic strain served as a template, owing to the interest of obtaining a scheme of immunization. Afterward, we performed enzyme-linked immunosorbent assay (ELISA) using the epitope to analyze if any antibodies in human sera before and after the influenza outbreak in 2009 recognize this peptide. Also, a plaque reduction neutralization test induced by virus-neutralizing antibodies and the IgG determination showed the biological activity of this computationally designed peptide. The results of the ELISAs demonstrated that the serum of both prepandemic and pandemic recognized the epitope. Moreover, the plaque reduction neutralization test evidenced the capacity of the designed peptide to neutralize influenza virus in Madin-Darby canine cells.

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“…To examine the ability of the two epitopes identified in this study to induce antibody responses, arginine-glycine-aspartate [40] was added on the N-terminal side of peptide aa 243–249 (RS-15), and an overlay of peptide aa 243–249 (YT-16) and peptide aa 243–262 (YV-20) were used to immunize mice. The epitopes were coupled with KLH and named RS-15-KLH, YT-16-KLH, and YV-20-KLH, respectively.…”

Section: Resultsmentioning

confidence: 99%

Characterization of an Immunodominant Epitope in the Endodomain of the Coronavirus Membrane Protein

Dong

Zhang

Shi

et al. 2016

Viruses

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The coronavirus membrane (M) protein acts as a dominant immunogen and is a major player in virus assembly. In this study, we prepared two monoclonal antibodies (mAbs; 1C3 and 4C7) directed against the transmissible gastroenteritis virus (TGEV) M protein. The 1C3 and 4C7 mAbs both reacted with the native TGEV M protein in western blotting and immunofluorescence (IFA) assays. Two linear epitopes, 243YSTEART249 (1C3) and 243YSTEARTDNLSEQEKLLHMV262 (4C7), were identified in the endodomain of the TGEV M protein. The 1C3 mAb can be used for the detection of the TGEV M protein in different assays. An IFA method for the detection of TGEV M protein was optimized using mAb 1C3. Furthermore, the ability of the epitope identified in this study to stimulate antibody production was also evaluated. An immunodominant epitope in the TGEV membrane protein endodomain was identified. The results of this study have implications for further research on TGEV replication.

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A novel method for enhancement of peptide vaccination utilizing T-cell epitopes from conventional vaccines

Cited by 12 publications

References 16 publications

The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein

The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein

A continuous peptide epitope reacting with pandemic influenza AH1N1 predicted by bioinformatic approaches

Characterization of an Immunodominant Epitope in the Endodomain of the Coronavirus Membrane Protein

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