About: Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry

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About: Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry
Creator	Zhao, Xuesen Zhang, Chengsheng Feng, Yan Lin, Han-Xin Tu, Xinming Griffin, Lauren Hsieh, Chih-Heng Junop, Murray
Source	Elsevier; Medline; PMC
abstract	Abstract The spike (S) protein of human coronavirus NL63 (HCoV-NL63) mediates both cell attachment by binding to its receptor hACE2 and membrane fusion during virus entry. We have previously identified the receptor-binding domain (RBD) and residues important for RBD–hACE2 association. Here, we further characterized the S protein by investigating the roles of the cytoplasmic tail and 19 residues located in the RBD in protein accumulation, receptor binding, and pseudotype virus entry. For these purposes, we first identified an entry-efficient S gene template from a pool of gene variants and used it as a backbone to generate a series of cytoplasmic tail deletion and single residue substitution mutants. Our results showed that: (i) deletion of 18aa from the C-terminus enhanced the S protein accumulation and virus entry, which might be due to the deletion of intracellular retention signals; (ii) further deletion to residue 29 also enhanced the amount of S protein on the cell surface and in virion, but reduced virus entry by 25%, suggesting that residues 19–29 contributes to membrane fusion; (iii) a 29aa-deletion mutant had a defect in anchoring on the plasma membrane, which led to a dramatic decrease of S protein in virion and virus entry; (iv) a total of 15 residues (Y498, V499, V531, G534, G537, D538, S540, G575, S576, E582, W585, Y590, T591, V593 and G594) within RBD were important for receptor binding and virus entry. They probably form three receptor binding motifs, and the third motif is conserved between NL63 and SARS-CoV.
has issue date	2011-09-30(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2011.06.029
bibo:pmid	21798295
has license	els-covid
sha1sum (hex)	bf500c9cbe8d702be5d0a459ae1136c9bbffc114
schema:url	https://doi.org/10.1016/j.virusres.2011.06.029
resource representing a document's title	Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry
has PubMed Central identifier	PMC7114368
has PubMed identifier	21798295
schema:publication	Virus Research
resource representing a document's body	covid:bf500c9cbe8d702be5d0a459ae1136c9bbffc114#body_text
is schema:about of	named entity 'PROTEIN ' named entity 'SPIKE PROTEIN' named entity 'CHARACTERIZATION' named entity 'accumulation' named entity 'signals' named entity 'protein' named entity 'protein' named entity 'motifs' named entity 'PROBABLY' named entity '28I' named entity 'TOTAL' named entity 'MUTANT' named entity 'PROTEIN ACCUMULATION' named entity 'MOTIF' named entity 'MOTIFS' named entity 'EFFICIENT' named entity 'HERE' named entity 'BINDING' named entity 'BACKBONE' named entity 'VIRUS ENTRY' named entity 'IDENTIFIED' named entity 'THESE' named entity 'ITS' named entity 'MIGHT BE' named entity 'RBD' named entity 'HACE2' named entity 'SPIKE' named entity 'INVESTIGATING' named entity 'SARS-COV' named entity 'CELL ATTACHMENT' named entity 'LOCATED IN' named entity 'GENE' named entity 'DECREASE' named entity 'PREVIOUSLY' named entity 'VARIANTS' named entity 'GENERATE' named entity 'RESULTS' named entity 'POOL' named entity 'ENHANCED' named entity 'DUE TO' named entity 'FORM' named entity 'ANCHORING' named entity 'VIRION' named entity 'RESIDUE' named entity 'PSEUDOTYPE VIRUS' named entity 'CHARACTERIZED' named entity 'HAVE' named entity 'PROTEIN ' named entity 'ASSOCIATION' named entity 'ROLES' named entity 'PLASMA MEMBRANE' named entity 'CONSERVED' named entity 'SERIES' named entity 'REDUCED' named entity 'BUT' named entity 'CYTOPLASMIC TAIL' named entity 'LED' named entity 'SUBSTITUTION' named entity 'NL63' named entity 'MUTANTS' named entity '28S' named entity 'CELL SURFACE' named entity 'RECEPTOR BINDING' named entity 'VIRUS ENTRY' named entity 'PSEUDOTYPE VIRUS' named entity 'OUR' named entity 'SIGNALS' named entity 'ENTRY' named entity 'THE CELL' named entity 'SINGLE' named entity 'INTRACELLULAR RETENTION' named entity 'PURPOSES' named entity 'RECEPTOR BINDING' named entity 'RECEPTOR'

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