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Juan Pedro Laclette - One of the best experts on this subject based on the ideXlab platform.

  • Epitope Mapping on n terminal region of taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Abstract Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host–parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region.

  • Epitope Mapping on N-terminal region of Taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host-parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region. Copyright (C) 2000 Elsevier Science B.V.

Takuya Ueda - One of the best experts on this subject based on the ideXlab platform.

  • Epitope Mapping using ribosome display in a reconstituted cell free protein synthesis system
    Journal of Biochemistry, 2009
    Co-Authors: Eriko Osada, Takashi Kanamori, Bintang K Akbar, Yoshihiro Shimizu, Takuya Ueda
    Abstract:

    Ribosome display is a powerful technology for selecting ligand-binding peptides or proteins. We demonstrate here that the ribosome display using the reconstituted cell-free protein synthesis system can be applied for the Epitope Mapping of monoclonal antibodies (mAbs). Using this technology, we selected peptides that specifically bind to three mAbs from random peptide library. When selection was performed against the anti-FLAG M2 antibody, selected peptides contained previously characterized consensus Epitope, indicating that the methodology can be applied for the Epitope Mapping. When the selection was carried out against two anti-beta-Catenin (anti-beta-Cat) mAbs, selected peptides had a homology for the partial peptide sequences of beta-Cat. Western blot analysis showed that these putative Epitopes had affinity for the corresponding mAbs and beta-Cat mutants that lack these regions did not bind to the antibodies, indicating we correctly mapped the Epitope for these mAbs. The study shown here provides a way for the quick identification of the Epitope of mAbs.

  • Epitope Mapping Using Ribosome Display in a Reconstituted Cell-Free Protein Synthesis System
    Journal of Biochemistry, 2009
    Co-Authors: Eriko Osada, Takashi Kanamori, Bintang K Akbar, Yoshihiro Shimizu, Takuya Ueda
    Abstract:

    Ribosome display is a powerful technology for selecting ligand-binding peptides or proteins. We demonstrate here that the ribosome display using the reconstituted cell-free protein synthesis system can be applied for the Epitope Mapping of monoclonal antibodies (mAbs). Using this technology, we selected peptides that specifically bind to three mAbs from random peptide library. When selection was performed against the anti-FLAG M2 antibody, selected peptides contained previously characterized consensus Epitope, indicating that the methodology can be applied for the Epitope Mapping. When the selection was carried out against two anti-β-Catenin (anti-P-Cat) mAbs, selected peptides had a homology for the partial peptide sequences of p-Cat. Western blot analysis showed that these putative Epitopes had affinity for the corresponding mAbs and β-Cat mutants that lack these regions did not bind to the antibodies, indicating we correctly mapped the Epitope for these mAbs. The study shown here provides a way for the quick identification of the Epitope of mAbs.

Karlen G. Gazarian - One of the best experts on this subject based on the ideXlab platform.

  • Epitope Mapping on n terminal region of taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Abstract Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host–parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region.

  • Epitope Mapping on N-terminal region of Taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host-parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region. Copyright (C) 2000 Elsevier Science B.V.

Eriko Osada - One of the best experts on this subject based on the ideXlab platform.

  • Epitope Mapping using ribosome display in a reconstituted cell free protein synthesis system
    Journal of Biochemistry, 2009
    Co-Authors: Eriko Osada, Takashi Kanamori, Bintang K Akbar, Yoshihiro Shimizu, Takuya Ueda
    Abstract:

    Ribosome display is a powerful technology for selecting ligand-binding peptides or proteins. We demonstrate here that the ribosome display using the reconstituted cell-free protein synthesis system can be applied for the Epitope Mapping of monoclonal antibodies (mAbs). Using this technology, we selected peptides that specifically bind to three mAbs from random peptide library. When selection was performed against the anti-FLAG M2 antibody, selected peptides contained previously characterized consensus Epitope, indicating that the methodology can be applied for the Epitope Mapping. When the selection was carried out against two anti-beta-Catenin (anti-beta-Cat) mAbs, selected peptides had a homology for the partial peptide sequences of beta-Cat. Western blot analysis showed that these putative Epitopes had affinity for the corresponding mAbs and beta-Cat mutants that lack these regions did not bind to the antibodies, indicating we correctly mapped the Epitope for these mAbs. The study shown here provides a way for the quick identification of the Epitope of mAbs.

  • Epitope Mapping Using Ribosome Display in a Reconstituted Cell-Free Protein Synthesis System
    Journal of Biochemistry, 2009
    Co-Authors: Eriko Osada, Takashi Kanamori, Bintang K Akbar, Yoshihiro Shimizu, Takuya Ueda
    Abstract:

    Ribosome display is a powerful technology for selecting ligand-binding peptides or proteins. We demonstrate here that the ribosome display using the reconstituted cell-free protein synthesis system can be applied for the Epitope Mapping of monoclonal antibodies (mAbs). Using this technology, we selected peptides that specifically bind to three mAbs from random peptide library. When selection was performed against the anti-FLAG M2 antibody, selected peptides contained previously characterized consensus Epitope, indicating that the methodology can be applied for the Epitope Mapping. When the selection was carried out against two anti-β-Catenin (anti-P-Cat) mAbs, selected peptides had a homology for the partial peptide sequences of p-Cat. Western blot analysis showed that these putative Epitopes had affinity for the corresponding mAbs and β-Cat mutants that lack these regions did not bind to the antibodies, indicating we correctly mapped the Epitope for these mAbs. The study shown here provides a way for the quick identification of the Epitope of mAbs.

Charles B Shoemaker - One of the best experts on this subject based on the ideXlab platform.

  • Epitope Mapping on n terminal region of taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Abstract Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host–parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region.

  • Epitope Mapping on N-terminal region of Taenia solium paramyosin
    Immunology Letters, 2000
    Co-Authors: Karlen G. Gazarian, Tatiana G. Gazarian, Ricardo Hernández, Carlos F Solis, Charles B Shoemaker, Juan Pedro Laclette
    Abstract:

    Epitope Mapping of the amino-terminal 20aa sequence from Taenia solium paramyosin (TPmy), an immunodominant protein involved in the complex host-parasite relationship in human and porcine cysticercosis is reported. A 12-mer random peptide phage display library was screened with antibodies raised against a synthetic peptide corresponding to the amino-terminal 20aa sequence of TPmy, its highly immunodominant region. In total, 57 clones isolated in two panning conditions were analyzed, of which a single group of 14 sequences found in 25 clones shared a consensus motif showing structural similarity with the antigen Arg10-Thr16 region. Copyright (C) 2000 Elsevier Science B.V.