About: Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

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About: Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation 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	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Creator	Mcguire, Andrew Feng, Junli Pancera, Marie Hurlburt, Nicholas Stuart, Andrew Wan, Yu-Hsin
Source	BioRxiv; Medline; PMC; WHO
abstract	SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain (RBD). The structure reveals CV30’s epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding.
has issue date	2020-06-12(xsd:dateTime)
bibo:doi	10.1101/2020.06.12.148692
bibo:pmid	32577631
has license	cc-by-nc-nd
sha1sum (hex)	21001a3df894112d421057ec99c52191db5df04d
schema:url	https://doi.org/10.1101/2020.06.12.148692
resource representing a document's title	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
has PubMed Central identifier	PMC7301900
has PubMed identifier	32577631
schema:publication	bioRxiv
resource representing a document's body	covid:21001a3df894112d421057ec99c52191db5df04d#body_text
is schema:about of	named entity 'pandemic' named entity 'epitope' named entity 'Structural' named entity 'BASIS' named entity 'X-RAY' named entity 'HERE' named entity 'IS A' named entity 'ITS' named entity 'MONOCLONAL ANTIBODY' named entity 'COVID-19' named entity 'preventing' named entity 'binding' named entity 'betacoronavirus' named entity 'ACE2 receptor' named entity 'COVID-19 pandemic' named entity 'ACE2' named entity 'antibody' named entity 'RBD' named entity 'crystal structure' named entity 'heavy chain' named entity 'SARS-CoV-2' named entity 'B38' named entity 'amino acid sequence homology' named entity 'epitope' named entity 'hydrogen bonds' named entity 'antibodies' named entity 'CB6' named entity 'germline' named entity 'RBD' named entity 'ACE2' named entity 'Viral entry' named entity 'RBD' named entity 'germline' named entity 'RBD' named entity 'receptor binding' named entity 'humoral immune response' named entity 'PDB' named entity 'potency' named entity 'mAb' named entity 'antibody' named entity 'conformation' named entity 'CB6' named entity 'COVID' named entity 'ACE2' named entity 'class I fusion protein' named entity 'epitope' named entity 'affinity maturation' named entity 'antibodies' named entity 'RBD' named entity 'heavy chains' named entity 'germline' named entity 'SARS-CoV-2' named entity 'SARS' named entity 'SARS-CoV-2' named entity 'binding site' named entity 'interact' named entity 'binding mechanism' named entity 'cross-reactivity' named entity 'SARS-CoV-2' named entity 'heavy chain' named entity 'potency' named entity 'germline' named entity 'heavy chain' named entity 'CDR loops' named entity 'vaccine design' named entity 'antibodies' named entity 'potency' named entity 'RBD' named entity 'electrostatic' named entity 'March 2020' named entity 'genomes' named entity 'antibody' named entity 'binding mechanism' named entity 'epitope' named entity 'immune response' named entity 'nM 12'

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