About: The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity

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About: The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity 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	The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity
Creator	Zhang, Li Li, Xiaoyu Zhang, Linqi Zhang, Qi Liu, Shuo Li, Xuguang Wang, Meng Zhang, J Huang, Weijin Nie, Jianhui Wang, Youchun Lu, Qiong Wang, L Li, Qianqian Liu, Huan Zhang, C Li, L Li, Q Liu, H Liu, Q Sun, X Wang, W Zhang, Huang, X Hao, L Lu, M Hao, Huan Liu, Junkai Nie, Lingling Qin, Haiyang Sun, Qiyu Wu, Jiajing Zhao, Chenyan Zhao, S Linqi, Nie, H
Source	Elsevier; Medline; PMC
abstract	Summary The spike protein of SARS-CoV-2 has been undergoing mutations and is highly glycosylated. It is critically important to investigate the biological significance of these mutations. Here we investigated 80 variants and 26 glycosylation site modifications for the infectivity and reactivity to a panel of neutralizing antibodies and sera from convalescent patients. D614G, along with several variants containing both D614G and another amino acid change, were significantly more infectious. Most variants with amino acid change at receptor binding domain were less infectious but variants including A475V, L452R, V483A and F490L became resistant to some neutralizing antibodies. Moreover, the majority of glycosylation deletions were less infectious whilst deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of glycosylation for viral infectivity. Interestingly, N234Q was markedly resistant to neutralizing antibodies, whereas N165Q became more sensitive. These findings could be of value in the development of vaccine and therapeutic antibodies.
has issue date	2020-07-17(xsd:dateTime)
bibo:doi	10.1016/j.cell.2020.07.012
bibo:pmid	32730807
has license	els-covid
sha1sum (hex)	2848985084ce9a47e44cdbc61603a28aaf2712dd
schema:url	https://doi.org/10.1016/j.cell.2020.07.012
resource representing a document's title	The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity
has PubMed Central identifier	PMC7366990
has PubMed identifier	32730807
schema:publication	Cell
resource representing a document's body	covid:2848985084ce9a47e44cdbc61603a28aaf2712dd#body_text
is schema:about of	named entity 'infectivity' named entity 'mutations' named entity 'infectivity' named entity 'viral' named entity 'Neutralization' named entity 'Strains' named entity 'deletion' covid:arg/2848985084ce9a47e44cdbc61603a28aaf2712dd named entity 'majority' named entity 'N343' named entity 'panel' named entity 'infectivity' named entity 'antibodies' named entity 'glycosylation' named entity 'resistant' named entity 'protein' named entity 'spike' named entity 'N-glycan' named entity 'glycosylation' named entity 'N343' named entity 'glycosylation' named entity 'receptor binding domain' named entity 'amino acid' named entity 'glycosylated' named entity 'therapeutic antibodies' named entity 'infectivity' named entity 'pseudotyped viruses' named entity 'Site-directed mutagenesis' named entity 'pseudotyped viruses' named entity 'epitopes' named entity 'RNA virus' named entity 'pseudovirus' named entity 'virion' named entity 'novel-coronavirus' named entity 'mAb' named entity 'clone' named entity 'deletions' named entity 'RBD' named entity 'GISAID' named entity 'non-human primate' named entity 'amino acid' named entity 'antibodies' named entity 'receptor' named entity 'RBD' named entity 'amino acid' named entity 'glycosylation sites'

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