About: Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27

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About: Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27 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	Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27
Creator	Jiang, Liwei Wang, Dongli Wang, Xinquan Zhang, Linqi Zhang, Senyan Wang, Nianshuang Yu, Xiaojuan Cui, Ye Fu, Lili Li, Dongxia Li, Ziqiang Shi, Xuanlin
topic	covid:023af2216525c16fa52a75b99cc91ebb03e93107#this
Source	Medline; PMC
abstract	The recently reported Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe respiratory illness in humans with an approximately 30% mortality rate. The envelope spike glycoprotein on the surface of MERS-CoV mediates receptor binding, membrane fusion, and viral entry. We previously reported two human monoclonal antibodies that target the receptor binding domain (RBD) of the spike and exhibit strong neutralization activity against live and pesudotyped MERS-CoV infection. Here we determined the crystal structure of MERS-CoV RBD bound to the Fab fragment of MERS-27 antibody at 3.20 Å resolution. The MERS-27 epitope in the RBD overlaps with the binding site of the MERS-CoV receptor DPP4. Further biochemical, viral entry, and neutralization analyses identified two critical residues in the RBD for both MERS-27 recognition and DPP4 binding. One of the residues, Trp535, was found to function as an anchor residue at the binding interface with MERS-27. Upon receptor binding, Trp535 interacts with the N-linked carbohydrate moiety of DPP4. Thus, MERS-27 inhibits MERS-CoV infection by directly blocking both protein-protein and protein-carbohydrate interactions between MERS-CoV RBD and DPP4. These results shed light on the molecular basis of MERS-27 neutralization and will assist in the optimization of MERS-27 as a tool to combat MERS-CoV infection.
has issue date	2015-08-18(xsd:dateTime)
bibo:doi	10.1038/srep13133
bibo:pmid	26281793
has license	cc-by
sha1sum (hex)	023af2216525c16fa52a75b99cc91ebb03e93107
schema:url	https://doi.org/10.1038/srep13133
resource representing a document's title	Structural basis for the neutralization of MERS-CoV by a human monoclonal antibody MERS-27
has PubMed Central identifier	PMC4539535
has PubMed identifier	26281793
schema:publication	Sci Rep
resource representing a document's body	covid:023af2216525c16fa52a75b99cc91ebb03e93107#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/023af2216525c16fa52a75b99cc91ebb03e93107
is schema:about of	named entity 'membrane fusion' named entity 'binding' named entity 'RBD' named entity 'RBD' named entity 'bound' named entity 'MERS' named entity 'HUMAN' named entity 'FRAGMENT OF' named entity 'EPITOPE' named entity 'BINDING' named entity 'CARBOHYDRATE MOIETY' named entity 'MERS' named entity 'IDENTIFIED' named entity 'CRITICAL' named entity 'EXHIBIT' named entity 'FAB FRAGMENT' named entity 'THESE' named entity 'INFECTION' named entity 'ONE OF' named entity 'ACTIVITY' named entity 'ASSIST' named entity 'REPORTED' named entity 'RECOGNITION' named entity 'RECENTLY' named entity 'DOMAIN' named entity 'COMBAT' named entity 'OPTIMIZATION' named entity 'RESOLUTION' named entity 'BLOCKING' named entity 'PREVIOUSLY' named entity 'SEVERE' named entity 'TARGET' named entity 'DPP4' named entity 'INTERFACE' named entity 'MOLECULAR BASIS' named entity 'RBD' named entity 'FUNCTION' named entity 'HERE' named entity 'MERS' named entity 'DIRECTLY' named entity 'OVERLAPS WITH' named entity 'ANCHOR' named entity 'SITE OF' named entity 'VIRAL ENTRY' named entity 'PROTEIN ' named entity 'TOOL' named entity 'BOUND' named entity 'CAUSES' named entity 'SURFACE' named entity 'BASIS' named entity 'STRUCTURAL' named entity 'ENVELOPE' named entity 'MONOCLONAL ANTIBODIES' named entity 'APPROXIMATELY' named entity 'CRYSTAL STRUCTURE' named entity 'STRONG' named entity '30%' named entity 'INTERACTIONS' named entity 'BINDING SITE' named entity 'RESIDUE' named entity 'RECEPTOR' named entity 'MEMBRANE FUSION' named entity 'DETERMINED' named entity 'MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS' named entity 'RESULTS' named entity 'RECEPTOR BINDING' named entity 'MERS-COV' named entity 'MONOCLONAL ANTIBODY'

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