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HCOV-NL63 spike protein glycopeptides

ABSTRACT: HCoV-NL63 is a coronavirus that can cause severe lower respiratory tract infections requiring hospitalization. Of great interest is understanding the HCoV-NL63 coronavirus spike glycoprotein trimer, which is the conformational machine responsible for entry into host cells and the sole target of neutralizing antibodies during infection. We utilized an electron-transfer/higher energy collision dissociation ion fragmentation scheme (Frese, C. K. et al., 2013.) in combination with cryo-electron microscopy to resolve the extensive glycan shield that obstructs the protein surface. These glycans provide a structural framework to understanding the accessibility of the protein to antibodies.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Human Coronavirus Nl63 (ncbitaxon:277944)

SUBMITTER: David Veesler

PROVIDER: MSV000085098 | MassIVE | Fri Mar 13 01:53:00 GMT 2020

SECONDARY ACCESSION(S): PXD004557

REPOSITORIES: MassIVE

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Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy.

Walls Alexandra C AC Tortorici M Alejandra MA Frenz Brandon B Snijder Joost J Li Wentao W Rey Félix A FA DiMaio Frank F Bosch Berend-Jan BJ Veesler David D

Nature structural & molecular biology 20160912 10

The threat of a major coronavirus pandemic urges the development of strategies to combat these pathogens. Human coronavirus NL63 (HCoV-NL63) is an α-coronavirus that can cause severe lower-respiratory-tract infections requiring hospitalization. We report here the 3.4-Å-resolution cryo-EM reconstruction of the HCoV-NL63 coronavirus spike glycoprotein trimer, which mediates entry into host cells and is the main target of neutralizing antibodies during infection. The map resolves the extensive glyc ...[more]

PMID: 27617430

Similar Datasets

HCOV-NL63 spike protein glycopeptides

Project description:HCoV-NL63 is a coronavirus that can cause severe lower respiratory tract infections requiring hospitalization. Of great interest is understanding the HCoV-NL63 coronavirus spike glycoprotein trimer, which is the conformational machine responsible for entry into host cells and the sole target of neutralizing antibodies during infection. We utilized an electron-transfer/higher energy collision dissociation ion fragmentation scheme (Frese, C. K. et al., 2013.) in combination with cryo-electron microscopy to resolve the extensive glycan shield that obstructs the protein surface. These glycans provide a structural framework to understanding the accessibility of the protein to antibodies.

2016-09-27 | PXD004557 | Pride

LC-MS/MS EThcD of MERS-CoV and SARS-CoV S N-linked glycopeptides from recombinant spike ectodomains and whole MERS virions

Project description:Recent outbreaks of severe acute respiratory syndrome and Middle-East respiratory syndrome along with the threat of a future coronavirus pandemic underscore the importance of finding ways to neutralize these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors using cryo electron microscopy and characterized the site-specific N-linked glycan profile of the recombinant S proteins with LC-MS/MS using EThcD fragmentation. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered premature fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on the coronavirus fusion activation pathway which appears to take place through a receptor-driven ratcheting mechanism.

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Transcriptomic profiling of human corona virus (HCoV)-229E -infected human cells

Project description:Human coronaviruses (HCoVs) cause mild to severe respiratory infection. Most of the common cold illnesses are caused by one of four HCoVs, namely HCoV-229E, HCoV-NL63, HCoV-HKU1 and HCoV-OC43. Several studies have applied global transcriptomic methods to understand host responses to HCoV infection, with most studies focusing on the pandemic severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome CoV (MERS-CoV) and the newly emerging SARS-CoV-2. In this study, Next Generation Sequencing was used to gain new insights into cellular transcriptomic changes elicited by alphacoronavirus HCoV-229E. HCoV-229E-infected MRC5 cells showed marked downregulation of superpathway of cholesterol biosynthesis and eIF2 signaling pathways. Moreover, upregulation of cyclins, cell cycle control of chromosomal replication, and role of BRCA1 in DNA damage response, alongside downregulation of the cell cycle G1/S checkpoint, suggest that HCoV-229E favors S phase for viral infection. Intriguingly, more than 80% of key factors of cell innate immunity, interferon-stimulated genes (ISGs) and other transcripts of early antiviral response genes were downregulated early in HCoV-229E infection. This study will enhance our understanding of commonly circulating HCoVs and hopefully provide critical information about still-emerging coronaviruses.

2021-03-03 | GSE155986 | GEO

LC-MS/MS EThcD of MERS-CoV and SARS-CoV S N-linked glycopeptides from recombinant spike ectodomains and whole MERS virions

2020-03-13 | MSV000085097 | MassIVE

Human Liver Epithelial Cell Chromatin Accessibility Response to HCoV-229E Infection

Project description:The purpose of this experiment was to evaluate how wild-type Human coronavirus strain 229E (HCoV-229E) infection alters chromatin accessiblity in infected but not mock-infected samples.

2025-12-23 | GSE280627 | GEO

Inhibition of coronavirus HCoV-OC43 by targeting the eIF4F complex [A549]

Project description:This study reports a screen to identify putative inhibitors of the eIF4F complex for potential effects on blocking coronavirus replication, using HCoV-OC43 (OC43) infection of Vero E6 cells and the lung epithelial cancer line A549 as models.

2022-12-13 | GSE198398 | GEO

Inhibition of coronavirus HCoV-OC43 by targeting the eIF4F complex [Vero E6]

2022-12-13 | GSE198399 | GEO

Human Primary Airway Epithelium Response to HCoV-229E Infection

Project description:The purpose of this experiment was to evaluate the human host cellular response to wild-type Human coronavirus strain 229E (HCoV-229E) infection. Sample data was obtained for mock and infected (MOI 3) primary human airway epithelial cells grown in air-liquid interface conditions, processed for RNA sequencing (RNA-Seq) expression analysis.

2025-10-01 | GSE279463 | GEO

HCoV-229E infection of the human HuH7 cell line [Experiment B]

Project description:The aim of the experiment is to identify changes in host gene expression upon infection of Huh7 hepatoma carcinoma cells with human coronavirus HCoV-229E as compared to uninfected cells and in comparison to cells stimulated by IL-1alpha (10ng/ml) for 1h. All experiments have been performed at 33°C which is required for sufficient viral entry/replication. Also included are two samples which have been treated with a heat inactivated coronavirus (56°C for 5min).

2017-03-15 | GSE89166 | GEO

Human A549 and MRC5 Cell Response to HCoV-229E Infection

Project description:The purpose of this experiment was to evaluate the human host cellular response to wild-type Human coronavirus strain 229E (HCoV-229E) infection. Sample data was obtained for mock and infected (MOI 5) immortalized human lung epithelial cells (A549) and immortalized human lung fibroblasts cells (MRC5) processed for RNA sequencing (RNA-Seq) expression analysis.

2025-10-01 | GSE279271 | GEO

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