Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F20%3A00538602" target="_blank" >RIV/60077344:_____/20:00538602 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14740/20:00114734 RIV/00027162:_____/20:N0000107

Výsledek na webu

<a href="https://www.nature.com/articles/s41598-020-70082-2" target="_blank" >https://www.nature.com/articles/s41598-020-70082-2</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-020-70082-2" target="_blank" >10.1038/s41598-020-70082-2</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells

Popis výsledku v původním jazyce

Tick-borne encephalitis virus (TBEV) is the causative agent of severe human neuroinfections that most commonly occur after a tick bite. N-Glycosylation of the TBEV envelope (E) glycoprotein is critical for virus egress in mammalian cells, but not in tick cells. In addition, glycans have been reported to mask specific antigenic sites from recognition by neutralizing antibodies. In this regard, the main purpose of our study was to investigate the profile of N-glycans linked to the E protein of TBEV when grown in human neuronal cells and compare it to the profile of virus grown in tick cells. Mass spectrometric analysis revealed significant differences in these profiles. High-mannose glycan with five mannose residues (Man(5)GlcNAc(2)), a complex biantennary galactosylated structure with core fucose (Gal(2)GlcNAc(2)Man(3)GlcNAc(2)Fuc), and a group of hybrid glycans with the composition Gal(0-1)GlcNAc(1)Man(3-5)GlcNAc(2)Fuc(0-1) were confirmed as the main asparagine-linked oligosaccharides on the surface of TBEV derived from human neuronal cells. The observed pattern was supported by examination of the glycopeptides, providing additional information about the glycosylation site in the E protein. In contrast, the profile of TBEV grown in tick cells showed that paucimannose (Man(3-4)GlcNAc(2)Fuc(0-1)) and high-mannose structures with five and six mannoses (Man(5-6)GlcNAc(2)) were major glycans on the viral surface. The reported results complement existing crystallography and cryoelectron tomography data on the E protein structure and could be instrumental for designing carbohydrate-binding antiviral agents active against TBEV.

Název v anglickém jazyce

Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells

Popis výsledku anglicky

Tick-borne encephalitis virus (TBEV) is the causative agent of severe human neuroinfections that most commonly occur after a tick bite. N-Glycosylation of the TBEV envelope (E) glycoprotein is critical for virus egress in mammalian cells, but not in tick cells. In addition, glycans have been reported to mask specific antigenic sites from recognition by neutralizing antibodies. In this regard, the main purpose of our study was to investigate the profile of N-glycans linked to the E protein of TBEV when grown in human neuronal cells and compare it to the profile of virus grown in tick cells. Mass spectrometric analysis revealed significant differences in these profiles. High-mannose glycan with five mannose residues (Man(5)GlcNAc(2)), a complex biantennary galactosylated structure with core fucose (Gal(2)GlcNAc(2)Man(3)GlcNAc(2)Fuc), and a group of hybrid glycans with the composition Gal(0-1)GlcNAc(1)Man(3-5)GlcNAc(2)Fuc(0-1) were confirmed as the main asparagine-linked oligosaccharides on the surface of TBEV derived from human neuronal cells. The observed pattern was supported by examination of the glycopeptides, providing additional information about the glycosylation site in the E protein. In contrast, the profile of TBEV grown in tick cells showed that paucimannose (Man(3-4)GlcNAc(2)Fuc(0-1)) and high-mannose structures with five and six mannoses (Man(5-6)GlcNAc(2)) were major glycans on the viral surface. The reported results complement existing crystallography and cryoelectron tomography data on the E protein structure and could be instrumental for designing carbohydrate-binding antiviral agents active against TBEV.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

13204

Kód UT WoS článku

000573234700005

EID výsledku v databázi Scopus

2-s2.0-85089155594