About: Differential Antibody Recognition by Novel SARS-CoV-2 and SARS-CoV Spike Protein Receptor Binding Domains: Mechanistic Insights and Implications for the Design of Diagnostics and Therapeutics

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About: Differential Antibody Recognition by Novel SARS-CoV-2 and SARS-CoV Spike Protein Receptor Binding Domains: Mechanistic Insights and Implications for the Design of Diagnostics and Therapeutics 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	Differential Antibody Recognition by Novel SARS-CoV-2 and SARS-CoV Spike Protein Receptor Binding Domains: Mechanistic Insights and Implications for the Design of Diagnostics and Therapeutics
Creator	Colombo, Giorgio Ilda D'annessa, Therapeutics Marchetti, Filippo
Source	BioRxiv
abstract	The appearance of the novel betacoronavirus SARS-CoV-2 represents a major threat to human health, and its diffusion around the world is causing dramatic consequences. The knowledge of the 3D structures of SARS-CoV-2 proteins can facilitate the development of therapeutic and diagnostic molecules. Specifically, comparative analyses of the structures of SARS-CoV-2 proteins and homologous proteins from previously characterized viruses, such as SARS-CoV, can reveal the common and/or distinctive traits that underlie the mechanisms of recognition of cell receptors and of molecules of the immune system. Herein, we apply our recently developed energy-based methods for the prediction of antibody-binding epitopes and protein-protein interaction regions to the Receptor Binding Domain (RBD) of the Spike proteins from SARS-CoV-2 and SARS-CoV. Our analysis focusses only on the study of the structure of RBDs in isolation, without making use of any previous knowledge of binding properties. Importantly, our results highlight structural and sequence differences among the regions that are predicted to be immunoreactive and bind/elicit antibodies. These results provide a rational basis to the observation that several SARS-CoV RDB-specific monoclonal antibodies fail to appreciably bind the SARS-CoV-2 counterpart. Furthermore, we correctly identify the region of SARS-CoV-2 RBD that is engaged by the cell receptor ACE2 during viral entry into host cells. The data, sequences and structures we present here can be useful for the development of novel therapeutic and diagnostic interventions.
has issue date	2020-03-15(xsd:dateTime)
bibo:doi	10.1101/2020.03.13.990267
has license	biorxiv
sha1sum (hex)	bde031fb77d6dc9c564f982e8646af6e8d87e46a
schema:url	https://doi.org/10.1101/2020.03.13.990267
resource representing a document's title	Differential Antibody Recognition by Novel SARS-CoV-2 and SARS-CoV Spike Protein Receptor Binding Domains: Mechanistic Insights and Implications for the Design of Diagnostics and Therapeutics
schema:publication	bioRxiv
resource representing a document's body	covid:bde031fb77d6dc9c564f982e8646af6e8d87e46a#body_text
is schema:about of	named entity 'cell receptors' named entity 'human health' named entity 'diffusion' named entity 'Antibody' named entity 'COMPARATIVE' named entity 'PREVIOUSLY' named entity 'APPEARANCE' named entity 'WORLD' named entity 'ITS' named entity 'STRUCTURES' named entity 'COMMON' named entity 'NOVEL' named entity 'causing' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'betacoronavirus' named entity 'SARS-CoV' named entity 'Mechanistic' named entity 'Insights' named entity 'Domains' named entity 'SARS-CoV-2' named entity 'SARS-CoV' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'Binding Domains' named entity 'SARS-CoV' named entity 'betacoronavirus' named entity 'three-dimensional structure' named entity 'interaction information' named entity 'spike proteins' named entity 'monoclonal antibodies' named entity 'spike protein' named entity 'crystal structures' named entity 'RBD' named entity 'Cryo-EM' named entity 'eigenvector' named entity 'Antibody' named entity 'eigenvalue' named entity 'SARS-CoV' named entity 'epitopes' named entity 'epitopes' named entity 'expasy' named entity 'antibodies' named entity 'Antibody' named entity 'RBD' named entity 'antibodies' named entity 'epidemics' named entity 'coronaviruses' named entity 'molecular probes' named entity 'Regione Lombardia' named entity 'SARS-CoV-2' named entity 'RBD' named entity 'SARS-CoV-2' named entity 'protein' named entity 'antibody' named entity 'solvation' named entity 'antibodies' named entity 'molecule' named entity 'immunological response' named entity 'GBSA' named entity 'SARS-CoV-2' named entity 'Monoclonal antibodies' named entity 'SARS-CoV-2' named entity 'epitopes' named entity 'epitope' named entity 'epitope' named entity 'GBSA' named entity 'Receptor Binding Domain' named entity 'receptor binding' named entity 'immunogens' named entity 'ACE2' named entity 'ACE2' named entity 'amino acids' named entity 'cell receptors' named entity 'epitopes' named entity 'protein' named entity 'virus' named entity 'protein' named entity 'mAbs' named entity '3.5' named entity 'protein' named entity 'efficaciously'

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