About: A humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: A humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.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 humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein
Creator	Yuen, Kwok-Yung Wu, Ying Lu, Guangwen Wang, Qihui Zhao, Jincun Perlman, Stanley Qi, Jianxun Yan, Jinghua Li, Yan Gao, George Liu, Wenjun Lu, Xuancheng Liu, Peipei Wan, Yuhua Zhang, Buchang
Source	Medline; PMC
abstract	The newly-emerging Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe and fatal acute respiratory disease in humans. Despite global efforts, the potential for an associated pandemic in the future cannot be excluded. The development of effective counter-measures is urgent. MERS-CoV-specific anti-viral drugs or vaccines are not yet available. Using the spike receptor-binding domain of MERS-CoV (MERS-RBD) to immunize mice, we identified two neutralizing monoclonal antibodies (mAbs) 4C2 and 2E6. Both mAbs potently bind to MERS-RBD and block virus entry in vitro with high efficacy. We further investigated their mechanisms of neutralization by crystallizing the complex between the Fab fragments and the RBD, and solved the structure of the 4C2 Fab/MERS-RBD complex. The structure showed that 4C2 recognizes an epitope that partially overlaps the receptor-binding footprint in MERS-RBD, thereby interfering with the virus/receptor interactions by both steric hindrance and interface-residue competition. 2E6 also blocks receptor binding, and competes with 4C2 for binding to MERS-RBD. Based on the structure, we further humanized 4C2 by preserving only the paratope residues and substituting the remaining amino acids with the counterparts from human immunoglobulins. The humanized 4C2 (4C2h) antibody sustained similar neutralizing activity and biochemical characteristics to the parental mouse antibody. Finally, we showed that 4C2h can significantly abate the virus titers in lungs of Ad5-hCD26-transduced mice infected with MERS-CoV, therefore representing a promising agent for prophylaxis and therapy in clinical settings.
has issue date	2015-09-22(xsd:dateTime)
bibo:doi	10.1038/cr.2015.113
bibo:pmid	26391698
has license	bronze-oa
sha1sum (hex)	8fb29b70a642337fe87dea06a8b8c0269e9bf50f
schema:url	https://doi.org/10.1038/cr.2015.113
resource representing a document's title	A humanized neutralizing antibody against MERS-CoV targeting the receptor-binding domain of the spike protein
has PubMed Central identifier	PMC4650419
has PubMed identifier	26391698
schema:publication	Cell Research
resource representing a document's body	covid:8fb29b70a642337fe87dea06a8b8c0269e9bf50f#body_text
is schema:about of	named entity 'RECEPTOR' named entity 'monoclonal antibodies' named entity 'interactions' named entity 'paratope' named entity 'development' named entity 'partially' named entity 'neutralizing antibody' named entity 'NEUTRALIZING ANTIBODY' named entity 'BINDING' named entity 'DOMAIN' named entity 'AMINO ACIDS' named entity 'HUMANIZED' named entity 'THERAPY' named entity 'RESIDUE' named entity 'MICE' named entity 'PARTIALLY' named entity 'MEASURES' named entity 'AGENT' named entity 'BIND' named entity 'BINDING' named entity 'DOMAIN' named entity 'RECEPTOR BINDING' named entity 'BASED' named entity 'COUNTER' named entity 'TARGETING' named entity 'ANTIBODY' named entity 'FRAGMENTS' named entity 'EFFECTIVE' named entity 'BLOCK' named entity 'STERIC HINDRANCE' named entity 'IDENTIFIED' named entity 'MERS-COV' named entity 'SPIKE PROTEIN' named entity 'HUMANIZED' named entity 'DEVELOPMENT' named entity 'OVERLAPS' named entity 'VIRUS ENTRY' named entity 'INVESTIGATED' named entity 'ACUTE RESPIRATORY DISEASE' named entity 'FAB' named entity 'RECEPTOR' named entity 'CLINICAL SETTINGS' named entity 'VIRAL' named entity 'HUMAN IMMUNOGLOBULINS' named entity 'PRESERVING' named entity 'VACCINES' named entity 'LUNGS' named entity 'CAUSE' named entity 'HIGH' named entity 'COMPLEX' named entity 'INTERACTIONS' named entity 'NEWLY' named entity 'PANDEMIC' named entity 'MOUSE' named entity 'FOOTPRINT' named entity 'MECHANISMS' named entity 'SEVERE' named entity 'AD5' named entity 'CHARACTERISTICS' named entity 'PARENTAL' named entity 'USING' named entity 'BIOCHEMICAL' named entity 'PROPHYLAXIS' named entity 'ACTIVITY' named entity 'EXCLUDED' named entity 'ABATE' named entity 'STRUCTURE'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software