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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Detalles Bibliográficos
Publicado: 2003
Materias:
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
Eukaryota
Trypanosoma
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v301_n4_p819_LopezBergami
http://hdl.handle.net/20.500.12110/paper_0006291X_v301_n4_p819_LopezBergami
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

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