About: A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures

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About: A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures
Creator	Denery-Papini, Sandra Larré, Colette Lollier, Virginie Tessier, Dominique
Source	Elsevier; Medline; PMC
abstract	Abstract Methods that predict antibody epitopes could help to promote the development of diagnostic tools, vaccines or immunotherapies by affecting the epitope binding of antibodies during an immunological response to antigens. It is generally assumed that there is a direct relationship between antibody accessibility to antigens and accessible surface of proteins. Based on this assumption, prediction systems often includes solvent accessibility values calculated from the primary sequence of proteins or from their three dimensional structures as a predictive criterion. However, the current prediction systems seem weakly efficient in view of benchmark tests. We were interested in evaluating how amino acids that have been experimentally identified as epitopic elements could differ from the rest of the antigenic molecule at the level of surface exposure, hence we assessed the average accessibility of epitopes. The approach used here utilises published epitopes deduced from numerous identification techniques, including sequence scanning and structure visualisation after crystallography, and it involves many types of antigens from toxins to allergens. Our results show that epitopic residues are not distributed among any specific Relative Surface Accessibility and Protrusion Index values and that, in some cases, epitopes cover the entire antigenic sequence. These results led to the conclusion that the classification of known epitopes with respect to the experimental conditions used to identify them should be introduced before attempting to characterise epitopic areas in a generic way.
has issue date	2011-01-31(xsd:dateTime)
bibo:doi	10.1016/j.molimm.2010.10.011
bibo:pmid	21111484
has license	els-covid
sha1sum (hex)	8fa08dbc9fa643cb18378ca35e1bad0a18454d20
schema:url	https://doi.org/10.1016/j.molimm.2010.10.011
resource representing a document's title	A generic approach to evaluate how B-cell epitopes are surface-exposed on protein structures
has PubMed Central identifier	PMC7112657
has PubMed identifier	21111484
schema:publication	Molecular Immunology
resource representing a document's body	covid:8fa08dbc9fa643cb18378ca35e1bad0a18454d20#body_text
is schema:about of	named entity 'promote' named entity 'B-cell' named entity 'APPROACH' named entity 'EXPOSED' named entity 'HELP' named entity 'TOOLS' named entity 'ANTIBODY' named entity 'AFFECTING' covid:arg/8fa08dbc9fa643cb18378ca35e1bad0a18454d20 named entity 'PREDICT' named entity 'DEVELOPMENT' named entity 'IMMUNOLOGICAL RESPONSE' named entity 'ANTIBODIES' named entity 'B-CELL' named entity 'METHODS' named entity 'DIAGNOSTIC' named entity 'EPITOPES' named entity 'HOW' named entity 'SURFACE' named entity 'PROTEIN STRUCTURES' named entity 'GENERIC' named entity 'BINDING' named entity 'EVALUATE' named entity 'IMMUNOTHERAPIES' named entity 'RESPONSE TO ANTIGENS' named entity 'VACCINES' named entity 'PROMOTE' named entity 'EPITOPES' named entity 'EPITOPE' named entity 'tools' named entity 'development' named entity 'epitopes' named entity 'immunotherapies' named entity 'structures' named entity 'protein' named entity 'epitopes' named entity 'antigens' named entity 'immunological response' named entity 'diagnostic tools' named entity 'protein structures' named entity 'amino acids' named entity 'epitopes' named entity 'epitopes' named entity 'antibody' named entity 'epitopes' named entity 'conformer' named entity 'amino acids' named entity 'synthetic peptide' named entity 'pattern matching' named entity 'epitopes' named entity 'diagnostic tools' named entity 'epitopes' named entity 'RSA' named entity 'viral proteins' named entity 'autoimmune' named entity 'epitope' named entity 'antibody' named entity 'PDB' named entity 'RSA' named entity 'epitopes' named entity 'amino acids' named entity 'protein sequences' named entity 'protein' named entity 'allergic response' named entity 'antigen' named entity 'myoglobin' named entity 'secondary structure' named entity 'RSA' named entity 'adsorption' named entity '3D structure' named entity 'antigen' named entity 'amino acid' named entity 'epitopes' named entity 'house dust mite' named entity 'protein sequences' named entity 'epitope' named entity 'multiple sclerosis' named entity 'epitopes'

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