Comparative properties of two peptide–antibody interactions as deduced from epitope delineation

Autor: Claude Granier, Laurence Choulier, Danièle Altschuh, Myriam Ben Khalifa, Etienne Weiss, Daniel Laune, Philippe Robinson, Georges Orfanoudakis
Přispěvatelé: Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), UMR 9921, CNRS/UM1, Modélisation et ingéniérie des systèmes complexes pour le diagnostic (MISCD), BIO-RAD FRANCE HOLDING-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2002
Předmět:
MESH: Epitopes
Phage display
030303 biophysics
Immunology
Peptide
Epitope
MESH: Antibodies
Monoclonal
Antigen-Antibody Reactions
Bacteriophage
Epitopes
Mice
03 medical and health sciences
chemistry.chemical_compound
MESH: Papillomaviridae
Antibody Specificity
Peptide Library
Peptide synthesis
MESH: Antigen-Antibody Reactions
Animals
Humans
Immunology and Allergy
MESH: Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH: Antibody Specificity
Peptide library
MESH: Mice
Papillomaviridae
030304 developmental biology
chemistry.chemical_classification
MESH: Epitope Mapping
0303 health sciences
MESH: Humans
biology
Linear epitope
MESH: Peptides
Antibodies
Monoclonal
Oncogene Proteins
Viral
biology.organism_classification
Epitope mapping
Biochemistry
chemistry
MESH: Oncogene Proteins
Viral
MESH: Peptide Library
Peptides
Epitope Mapping
Zdroj: Journal of Immunological Methods
Journal of Immunological Methods, Elsevier, 2002, 259 (1-2), pp.77-86. ⟨10.1016/S0022-1759(01)00496-3⟩
Journal of Immunological Methods, Elsevier, 2002, 259 (1-2), pp.77-86
ISSN: 0022-1759
DOI: 10.1016/s0022-1759(01)00496-3
Popis: The linear epitope recognized by three closely related antibodies specific for the E6 oncoprotein of papillomavirus type 16 was delineated by phage display, spot peptide synthesis on cellulose membranes, and kinetic measurements with antigenic variants using a BIACORE. The same approaches, recently applied to an antibody specific for tobacco mosaic virus protein, led to the clear-cut delineation of a functional epitope comprising four key positions with well defined physico-chemical properties. In contrast, the E6 system is characterized by a non-essential contribution to binding of various factors, so that combinations of alternative properties are compatible with measurable binding activity.
Databáze: OpenAIRE
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