Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins
The variable genes of monoclonal antibody (mAb) B10, specific for the C-terminal region of the eukaryotic ribosomal P protein, have been cloned as a single-chain Fv fragment (scFv) and expressed in Escherichia coli. The primary sequence of the variable regions of the B10 antibody, together with a de...
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todo:paper_0006291X_v301_n4_p819_LopezBergami2023-10-03T14:03:49Z Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins López Bergami, P. Mateos, P. Hoebeke, J. Levin, M.J. Baldi, A. Autoantibody Paratope-epitope modelling Ribosomal P protein Single-chain Fv fragment Trypanosoma cruzi autoantibody epitope monoclonal antibody ribosome protein antibody combining site article binding affinity carboxy terminal sequence Escherichia coli eukaryote molecular biology molecular cloning molecular interaction nonhuman nucleotide sequence priority journal protein analysis protein expression sequence analysis Escherichia coli Eukaryota Trypanosoma Trypanosoma cruzi The variable genes of monoclonal antibody (mAb) B10, specific for the C-terminal region of the eukaryotic ribosomal P protein, have been cloned as a single-chain Fv fragment (scFv) and expressed in Escherichia coli. The primary sequence of the variable regions of the B10 antibody, together with a detailed characterization of the reactive residues of the antigen, allowed the construction of a model of the paratope-epitope interaction, giving a first insight into the binding mechanisms of anti-P autoantibodies to their target peptides. The mAb and scFv could be useful for extensive P protein detection since both recognize the highly conserved motif DDxGF. © 2003 Elsevier Science (USA). All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v301_n4_p819_LopezBergami |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Autoantibody Paratope-epitope modelling Ribosomal P protein Single-chain Fv fragment Trypanosoma cruzi autoantibody epitope monoclonal antibody ribosome protein antibody combining site article binding affinity carboxy terminal sequence Escherichia coli eukaryote molecular biology molecular cloning molecular interaction nonhuman nucleotide sequence priority journal protein analysis protein expression sequence analysis Escherichia coli Eukaryota Trypanosoma Trypanosoma cruzi |
spellingShingle |
Autoantibody Paratope-epitope modelling Ribosomal P protein Single-chain Fv fragment Trypanosoma cruzi autoantibody epitope monoclonal antibody ribosome protein antibody combining site article binding affinity carboxy terminal sequence Escherichia coli eukaryote molecular biology molecular cloning molecular interaction nonhuman nucleotide sequence priority journal protein analysis protein expression sequence analysis Escherichia coli Eukaryota Trypanosoma Trypanosoma cruzi López Bergami, P. Mateos, P. Hoebeke, J. Levin, M.J. Baldi, A. Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
topic_facet |
Autoantibody Paratope-epitope modelling Ribosomal P protein Single-chain Fv fragment Trypanosoma cruzi autoantibody epitope monoclonal antibody ribosome protein antibody combining site article binding affinity carboxy terminal sequence Escherichia coli eukaryote molecular biology molecular cloning molecular interaction nonhuman nucleotide sequence priority journal protein analysis protein expression sequence analysis Escherichia coli Eukaryota Trypanosoma Trypanosoma cruzi |
description |
The variable genes of monoclonal antibody (mAb) B10, specific for the C-terminal region of the eukaryotic ribosomal P protein, have been cloned as a single-chain Fv fragment (scFv) and expressed in Escherichia coli. The primary sequence of the variable regions of the B10 antibody, together with a detailed characterization of the reactive residues of the antigen, allowed the construction of a model of the paratope-epitope interaction, giving a first insight into the binding mechanisms of anti-P autoantibodies to their target peptides. The mAb and scFv could be useful for extensive P protein detection since both recognize the highly conserved motif DDxGF. © 2003 Elsevier Science (USA). All rights reserved. |
format |
JOUR |
author |
López Bergami, P. Mateos, P. Hoebeke, J. Levin, M.J. Baldi, A. |
author_facet |
López Bergami, P. Mateos, P. Hoebeke, J. Levin, M.J. Baldi, A. |
author_sort |
López Bergami, P. |
title |
Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
title_short |
Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
title_full |
Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
title_fullStr |
Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
title_full_unstemmed |
Sequence analysis, expression, and paratope characterization of a single-chain Fv fragment for the eukaryote ribosomal P proteins |
title_sort |
sequence analysis, expression, and paratope characterization of a single-chain fv fragment for the eukaryote ribosomal p proteins |
url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v301_n4_p819_LopezBergami |
work_keys_str_mv |
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