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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Autores principales: López Bergami, P., Mateos, P., Hoebeke, J., Levin, M.J., Baldi, A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v301_n4_p819_LopezBergami
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spelling 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
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