About: Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics

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

About: Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics 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	Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics
Creator	Zhang, Wen Peng, Chao Tian, Xiaoxu Ruibingqi, Zhou, Dapeng
Source	Medline; PMC
abstract	Coronaviruses hijack human enzymes to assemble the sugar coat on their spike glycoproteins. The mechanisms by which human antibodies may recognize the antigenic viral peptide epitopes hidden by the sugar coat are unknown. Glycosylation by insect cells differs from the native form produced in human cells, but insect cell–derived influenza vaccines have been approved by the US Food and Drug Administration. In this study, we analyzed recombinant severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein secreted from BTI-Tn-5B1–4 insect cells, by trypsin and chymotrypsin digestion followed by mass spectrometry analysis. We acquired tandem mass spectrometry (MS/MS) spectrums for glycopeptides of all 22 predicted N-glycosylated sites. We further analyzed the surface accessibility of spike proteins according to cryogenic electron microscopy and homolog-modeled structures, and available antibodies that bind to SARS-CoV-1. All 22 N-glycosylated sites of SARS-CoV-2 are modified by high-mannose N-glycans. MS/MS fragmentation clearly established the glycopeptide identities. Electron densities of glycans cover most of the spike receptor-binding domain of SARS-CoV-2, except YQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQ, similar to a region FSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQ in SARS-CoV-1. Other surface-exposed domains include those located on central helix, connecting region, heptad repeats, and N-terminal domain. Because the majority of antibody paratopes bind to the peptide portion with or without sugar modification, we propose a snake-catching model for predicted paratopes: a minimal length of peptide is first clamped by a paratope, and sugar modifications close to the peptide either strengthen or do not hinder the binding.
has issue date	2020-06-10(xsd:dateTime)
bibo:doi	10.1093/glycob/cwaa052
bibo:pmid	32518941
has license	no-cc
sha1sum (hex)	b4d87c8e68bb1fc101f14d3be490fa6142e413b8
schema:url	https://doi.org/10.1093/glycob/cwaa052
resource representing a document's title	Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics
has PubMed Central identifier	PMC7313968
has PubMed identifier	32518941
schema:publication	Glycobiology
resource representing a document's body	covid:b4d87c8e68bb1fc101f14d3be490fa6142e413b8#body_text
is schema:about of	named entity 'enzymes' named entity 'glycopeptide' named entity 'accessible' named entity 'Identification' named entity 'glycoproteins' named entity 'enzymes' named entity 'vaccination' named entity 'receptor' named entity 'adjuvant' named entity 'receptor' named entity 'SARS-CoV-2' named entity 'tyrosine' named entity 'helix' named entity 'alkylate' named entity 'vaccine' named entity 'chymotrypsin' named entity 'sugar' named entity 'glycopeptide' named entity 'ah1' named entity 'epitopes' named entity 'MAbs' named entity 'binding domains' named entity 'N-glycosylation' named entity 'Middle East respiratory syndrome' named entity 'glycosylated' named entity 'SARS-CoV-1' named entity 'glycopeptide' named entity 'Protein Data Bank' named entity 'Middle East respiratory syndrome coronavirus' named entity 'N-glycosylation' named entity 'SARS-CoV' named entity 'coronaviruses' named entity 'homolog' named entity 'vaccine design' named entity 'helix' named entity 'glycopeptides' named entity 'MS/MS' named entity 'Asn' named entity 'Glycome' named entity 'therapeutic effects' named entity 'epitopes' named entity 'SARS-CoV-1' named entity 'N343' named entity 'Achilles heel' named entity 'MAbs' named entity 'glycans' named entity 'glycans' named entity '4D5' named entity 'GlcNAc' named entity 'peptide' named entity 'human immunodeficiency virus 1' named entity 'epitope' named entity 'spike proteins' named entity 'N-terminal' named entity 'epitopes' named entity 'receptor' named entity 'ah2' named entity 'ACE2' named entity 'SARS-CoV-2' named entity 'Wen Zhang' named entity 'receptor' named entity 'glycans' named entity 'glycoproteins' named entity 'binding sites' named entity 'Achilles heel' named entity 'furin' named entity 'glycoproteins' named entity 'peptide' named entity 'lung' named entity 'GlcNAc' named entity 'SWISS-MODEL' named entity 'chymotrypsin' named entity 'homology' named entity 'heptad repeat' named entity 'virus' named entity 'adjuvants' named entity 'SARS-CoV-2'

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